Enzymes From Rare Actinobacterial Strains

CHAPTER FOUR

Enzymes From Rare Actinobacterial Strains J. Suriya*, S. Bharathiraja†, P. Manivasagan{, S.-K. Kim{,§,1 *School of Environmental Sciences, Bharathidasan University, Tiruchirappalli, Tamil Nadu, India † CAS in Marine Biology, Annamalai University, Porto Novo, Tamil Nadu, India { Marine Bioprocess Research Center, Pukyong National University, Busan, Republic of Korea § Specialized Graduate School Science & Technology Convergence, Pukyong National University, Busan, Republic of Korea 1 Corresponding author: e-mail addresses: [email protected]; [email protected]

Contents 1. Introduction 2. Rare Actinomycetes and Selective Isolation 3. Various Types of Actinobacterial Enzymes 3.1 Extremophilic Enzymes From Actinobacteria 3.2 Oxidative Enzymes From Actinobacteria 3.3 Lignocellulolytic Enzymes From Actinobacteria 3.4 Other Industrially Important Actinobacterial Enzymes 4. Conclusion Acknowledgments References

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Abstract Actinobacteria constitute rich sources of novel biocatalysts and novel natural products for medical and industrial utilization. Although actinobacteria are potential source of economically important enzymes, the isolation and culturing are somewhat tough because of its extreme habitats. But now-a-days, the rate of discovery of novel compounds producing actinomycetes from soil, freshwater, and marine ecosystem has increased much through the developed culturing and genetic engineering techniques. Actinobacteria are well-known source of their bioactive compounds and they are the promising source of broad range of industrially important enzymes. The bacteria have the capability to degrade a range of pesticides, hydrocarbons, aromatic, and aliphatic compounds (Sambasiva Rao, Tripathy, Mahalaxmi, & Prakasham, 2012). Most of the enzymes are mainly derived from microorganisms because of their easy of growth, minimal nutritional requirements, and low-cost for downstream processing. The focus of this review is about the new, commercially useful enzymes from rare actinobacterial strains. Industrial requirements are now fulfilled by the novel actinobacterial enzymes which assist the effective production. Oxidative enzymes, lignocellulolytic enzymes,

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extremozymes, and clinically useful enzymes are often utilized in many industrial processes because of their ability to catalyze numerous reactions. Novel, extremophilic, oxidative, lignocellulolytic, and industrially important enzymes from rare Actinobacterial population are discussed in this chapter.

1. INTRODUCTION Actinobacteria are primarily saprophytes which remarkably contribute in the turnover of complex biopolymers such as pectin, hemicellulose, keratin, lignocellulose, and chitin. In addition to this, they are also a good resource of antibiotics, enzymes, and other bioactive molecules. Henceforth they are utilized in pharmaceutical and other industries (Stutzenberger & Berdine, 1992). Among the other microorganisms, actinobacteria received much attention due to their production of wide range of biologically active compounds. Chemical reactions are catalyzed by enzymes which can be classified into intracellular and extracellular enzymes based on their origin (Baldrian, 2014). Due to high yield, cost efficiency, and susceptibility to genetic manipulation, microorganisms are mostly preferred for enzyme production. Microbial enzymes have been extensively used in various industries like food, detergent, textile, pharmaceutical industries, and also in the fields of medical therapy, bioorganic chemistry, and molecular biology. Maximum production of commercial enzymes, pharmaceuticals, enzyme inhibitors, and antitumor agents has been obtained from Actinobacteria due its omnipresent nature (Remya & Vijayakumar, 2008). In recent years, numerous research works have been carried out to assess the marine actinobacterial diversity and its enzyme-producing capability in the unexplored marine sediments, hyper saline saltpan, and mangrove. The rare actinomycetes (nonstreptomycetes) are strains of actinomycetes whose isolation rate by culturable methods is much lesser than that of streptomycete strains (Seong, Choi, & Baikm, 2001). Physiology, basic knowledge of the habitats and secondary metabolite diversity of the rare actinomycetes has been gradually increased (Tiwari & Gupta, 2012). Different unexplored environments are targeted for the isolation of rare actinomycetes due to its potential in the production of enormous novel bioactive compounds. A 220 rare actinomycete genera have been isolated from unexplored habitats such as different marine sources (Goodfellow

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et al., 2012), hyper arids (Okoro et al., 2009), soil samples (Ara, Bakir, Hozzein, & Kudo, 2013), Volcanic zones (Lee & Lee, 2011), plant materials (Zhao et al., 2011), extreme saline zones (Jose & Jebakumar, 2013), glaciers (Zhang et al., 2012), and much more. Rare actinomycetes are the good sources of novel enzymes. The isolation of novel enzymes from these rare actinobacteria nourishes the current enzyme discovery programs. Oxidative enzymes are oxidoreductases that catalyze oxidation– reduction reactions. Interest toward the production of actinobacterial oxidative enzymes is increased much over the past 20 years particularly in the fields of lignin degradation and detoxification of organic pollutants, phosphate pesticides, and azo dyes (Pasti, Pometto, Nuti, & Crawford, 1990; Torres, Bustos-Jaimes, & Le Borgne, 2003). Various actinobacterial oxidative enzymes play an important role in morphogenesis or antibiotic production (Endo et al., 2003; Suzuki, Furusho, Higashi, Ohnishi, & Horinouchi, 2006). Lignocellulases are hydrolytic enzymes which are able to degrade tough lignocelluloses such as hemicellulases, cellulases, and lignolytic enzymes (Mtui, 2012) and are also utilized in various applications (Deswal, Sharma, Gupta, & Kuhad, 2012). Lignocelluloses are the abundant renewable biomass on earth (Isikgor & Becer, 2015). Lignocellulolytic enzymes can be produced from diverse types of microbes including fungi and bacteria (de-Souza, 2013). Compared with other bacteria, actinomycetes are an attractive group, being exploited for production of lignocellulases. Lignocellulolytic enzymes, one of the strong compounds delivered by actinomycetes, can be utilized generally as a part of different lignocelluloses based commercial enterprises (Prakash et al., 2013). Cellulases are used in biomethane and bioethanol production (Gupta, Samant, & Sahu, 2012), and also industries like textile industry, detergents industry, pulp and paper industry, animal feed, and food industry (Sukumaran, Singhania, & Pandey, 2005). Hemicellulases are applied in deinking of paper waste, biobleaching, up gradation of feed, fodder, and fibers, clarification of fruit juices, saccharification of hemicelluloses to xylose sugars (Soni & Kango, 2013). A wide range of enzymes useful in biotechnological industries and biomedical fields have been studied from various genus of actinobacteria. While there is essential information available due to the arrival of genomic and proteomic reports of actinobacteria has been constantly screened for the production of novel enzymes like proteases, chitinases, cellulases, xylanases, amylases, and other industrially important enzymes.

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2. RARE ACTINOMYCETES AND SELECTIVE ISOLATION Isolation of rare actinobacterial strains from the environment, culturing them in normal lab condition and maintenance of that isolates under suitable conditions are very hard and difficult which lead to the comparatively low occurrence of rare actinomycetes (Berdy, 2005). In order to overcome this problem, suitable isolation and selection procedures are required (Khanna, Solanki, & Lal, 2011; Qiu, Ruan, & Huang, 2008). Some necessary things have been kept in mind during the isolation of rare actinobacterial strains which include (i) employ appropriate selective media containing macromolecules such as chitin, casein, and humic acid for promotion of growth rate of rare actinomycetes and concurrently reduce contamination by bacterial/fungal colonies (Bredholdt, Fjaervik, Johnsen, & Zotchev, 2008; Cuesta, Garcia-de-la-Fuente, Abad, & Fornes, 2012; Hong et al., 2009; Qiu et al., 2008; Zhang & Zhang, 2011), (ii) by adding different antibiotics for fungal and bacteria to the media will enhance the selection of actinomycetales (Hong et al., 2009; Qiu et al., 2008; Zhang & Zhang, 2011), (iii) Sporulating actinobacterial strains are induced to produce motile spores and it is attained by applying chemoattractants like chloride, xylose, bromide, vanillin, and collidine for spore accumulation from actinoplanes (Hayakawa, 2008), (iv) from the application of different frequency of radiation, selective isolation of various kind of actinomycetes can be done (Bredholdt et al., 2007). SHF (super-high frequency) radiation allow effective isolation of Rhodococcus and Streptosporangium species, EHF (extremely high frequency) and UV radiation applied for efficient isolation of actinomycetes like Nocardiopsis, Nocardia, and Streptosporangium spp. (v) by applying chloramine treatment, Microtetraspora, Herbidospora, Streptosporangium, and Microbispora genera can be selectively isolated (Hong et al., 2009), (vi) for the isolation of marine actinomycetales Salinispora, seawater based media is used (Maldonado et al., 2005). Among numerous actinomycetes species, only 11 rare actinomycetes species producing 50 bioactive compounds altogether were identified in 1970 (Berdy, 2005). Today the number has reached nearly 100 of rare actinomycetes and the number is increasing due to the newly developed genetic and proper isolation techniques (Berdy, 2005; Bredholdt et al., 2007). The ability to produce potential new compounds will certainly make a way for the production of clinically important antibiotics (Anzai et al., 2008; Arumugam et al., 2009; Carlson, Li, Burr, & Sherman, 2009; Hohmann et al., 2009;

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Hong et al., 2009; Lam, 2006; Niu et al., 2007; Pimentel-Elardo et al., 2010; Rahman et al., 2010; Xu et al., 2010). Extremophiles produce extremozymes which have immense potential to work under harsh conditions, which were unsuitable for the normal enzymatic activity. Extremozymes are the promising alternatives for current industrial applications because which has optimal activity and stability under extreme conditions where as rare actinomyces are usually found and active in the common as well as uncommon environments but their isolation prevalence by culture dependent methods is much lesser than that of other actinomycetes strains.

3. VARIOUS TYPES OF ACTINOBACTERIAL ENZYMES Based on source, habitats, uses, and applications, here we divide the actinobacterial enzymes into some divisions for the easy and better understanding.

3.1 Extremophilic Enzymes From Actinobacteria Generally microbes are not restricted to specific environmental conditions. Microbial population can be found in the most diverse conditions, including extremes of pressure, temperature, pH, and salinity. These microorganisms known to be extremophiles, from which we can obtain biocatalysts and these are stable and functional at extreme conditions. Over the past years, industrial application of biocatalysts which can withstand at harsh environment has increased greatly. This is possible by the discovery of novel enzymes from extremophilic microbes from unusual extreme environments. Like other microorganisms, actinobacteria can survive in mesophilic, halophilic, acidophilic, and thermophilic conditions and they have the capability to degrade starch by hydrolysis (Williams et al., 1983). The mesophilic actinomyces genera Nocardia and Streptomyces produce amylases (Mordarski, Wieczorek, & Jaworska, 1970). Studies show that their enzymes are similar to bacillus amylases which are thermolabile. From the literature survey, Streptomyces hygroscopicus (McKillop, Elvin, & Kenten, 1986), S. limosus (Fairbairn, Priest, & Stark, 1986), and S. praecox (Suganuma, Mizukami, Moari, Ohnishi, & Hiromi, 1980) strains are more capable as amylase producers as a result of broad screening methods employed. High concentration of thermostable amylases was obtained from thermophilic actinobacteria, Thermomonospora curvata, T. vulgaris (Stutzenberger & Carnell, 1977; Stutzenberger, Kanno, Tamura, & Suekane, 1978) and from

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a Thermoactinomyces sp. (Obi & Obido, 1984a, 1984b). The compounds are relatively stable and highly active at 60–70°C and also stable at slightly acidic and neutral pH values (Kuo & Hartman, 1967). DyP-type peroxidase enzyme from the thermophilic actinomycete, Thermobifida fusca was isolated by Van Bloois, Torres-Pazmin˜o, Winter, and Fraaije (2010), which show maximum reactivity toward anthraquinone dyes, and sensible activity toward aromatic sulfides, standard peroxidase substrates, and azo dyes. In 2014, Jaouadi et al. isolated humic acid biodegrading peroxidase enzyme from Streptomyces albidoflavus which are highly thermophilic and exhibit higher catalytic efficiency than HRP (Jaouadi et al., 2014). Sutherland, Crawford, and Pometto (1981), when inducing the culture of four thermophilic Streptomyces with benzoic acids, observed high C12O activity. Thermotolerant enzymes obtained from actinobacteria are listed in Table 1. Marine Halophilic Actinobacteria Micromonospora, Streptomyces, and Rhodococcus are isolated from marine environment (Reiss, Ihssen, & Th€ ony-Meyer, 2011). They also isolated other group of actinomycetes which includes Dietzia, Marinophilus, Salinispora, Salinibacterium, Solwaraspora, Aeromicrobium, Gordonia, Microbacterium, Pseudonocardia, Actinomadura, Nocardiopsis, Saccharopolyspora, Nonomuraea, Williamsia, Streptosporangium, and Verrucosispora (Fernandes, da Silveira, Passos, & Zucchi, 2014a; Machczynski, Vijgenboom, Samyn, & Canters, 2004; Reiss et al., 2011). Endophytic Actinobacteria are inhabited at the internal part of plants, which helps in the protection of host plant against insects and various diseases. Generally, these endophytic actinobacteria are Streptomyces sp., Streptoverticillium, Micromonospora, Nocardia, Kitasatospora, Pseudonocardia, Nocardioides, Kibdelosporangium, Actinopolyspora, Brevibacterium, Actinomadura, Table 1 Some Extremozymes from Extremophilic Actinobacteria Enzyme Producers Enzyme Temperature (°C)

pH

Streptomycetes transformant T3-1

Cellulase

50

6.5

Streptomyces rimosus R6-554W

Lipase

50

9.0–10.0

Thermomonospora fusca NTU22

α-Amylase

60

7.0

Thermomonospora fusca

Xylanase

60–80

7.0 (6–8)

Thermoactinomycetes sp. HS682

Protease

70

11.0

Thermomonospora sp.

Cellulase

60–70

6.0

Streptomyces antibiotius

Cellulase

40–55

5–7

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Glycomyces, Plantactinospora, Microbispora, Polymorphospora, Streptosporangium, and Promicromonospora which are found in the plants. Acidophilic Actinobacteria that generally grows at very low acidic pH range from 3.5 to 6.5 is found in acidic forest and mine drainage soil (Fernandes et al., 2014a; Ska´lova´ et al., 2009). Industrially important acidophilic enzymes are being obtained from the Streptomyces sp. and Kitasatospora.

3.2 Oxidative Enzymes From Actinobacteria Laccase, peroxidase, and tyrosinase are the important group of Oxidative enzymes which catalyses oligomerization, depolymerization, and hydroxylation reactions. Laccase and tyrosinase require molecular oxygen for catalyzing their reactions and produce water. Henceforth, these two enzymes are referred as “green enzymes.” Due to these catalyzing properties, oxidative enzymes are utilized in a variety of industrial processes. In the past decades, most oxidative enzymes were obtained from fungal species. But in recent years, it has become clear that these enzymes are well produced by actinobacterial strains, which are considered as an unexplored resource of oxidative enzymes with large number of industrial applications. 3.2.1 Cholesterol Oxidase Cholesterol oxidases (CO) are very useful enzymes for biotechnological applications because of its ability for the detection and conversion of cholesterol. Actinobacterial CO is being isolated from diverse environment and some of the rare actinomycetes like Corynebacterium spp., Streptomyces spp., Rhodococcus rhodochrous, Mycobacterium spp., Rhodococcus erythropolis, and Brevibacterium spp. are the major producers of the enzyme (MacLachlan, Wotherspoon, Ansell, & Brooks, 2000). Ivshina, Grishko, Nogovitsina, Kukina, and Tolstikov (2005) demonstrated the bioconversion of testosterone with the addition of glucose as cooxidant in the presence of the inhibitor 2,2ʹ-dipyridyl by cholesterol oxidase which is isolated from actinobacteria Rhodococcus strains. Now a days CO from actinobacteria are applied in analytical practices, like cholesterol measurement in biological fluids and to quantify the dehydroepiandrosterone sulfate (DHEAS) in cysts of the human mammary gland duct liquids (Donova, 2007). Streptomyces spp. producing cholesterol oxidases are used as a rich source of insecticidal proteins. Though actinobacterial cholesterol oxidase has more industrial applications, these also been concerned as a causative agent for human diseases. Actinobacterial strain Rhodococcus equi act as a primary pathogen for horses and requires cholesterol oxidase for opportunistic infection in humans

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which will cause membrane damage (Kumari & Kanwar, 2012). Brzostek, Dziadek, Rumijowska-Galewicz, Pawelczyk, and Dziadek (2007) confirmed the presence of another cholesterol oxidase which plays a main role in the M. tuberculosis pathogenesis. So from this we can get the idea about developing a treatment for the opportunistic infections by clearly understanding the virulence factors of cholesterol oxidase enzyme. 3.2.2 Peroxidases Peroxidases are a major group of oxidoreductases enzymes which can contain a heme cofactor in their active sites or redox-active selenocysteine or cysteine residues that catalyze the oxidation of substrate molecules by the hydrogen peroxide (H2O2) as the electron acceptor (Van Bloois et al., 2010). Actinobacteria are known to be a rich source of peroxidases, a novel industrially important enzyme, chiefly in a market which is dominated by the plant horseradish peroxidase (HRP) (Le Roes-Hill, Khan, & Burton, 2011; Mercer, Iqbal, Miller, & McCarthy, 1996; Tuncer, Rob, Ball, & Wilson, 1999). This HRP is the major enzyme for the removal of predominant pollutants such as phenols by enzyme-catalyzed polymerization reaction. It can be also used to alter toxic materials into a lesser amount of harmful substances. DyP type of peroxidase enzyme isolated by Van Bloois et al. (2010) from Thermobifida fusca, a thermophilic actinomycete, which showed high reactivity toward anthraquinone dyes. Many actinobacterial peroxidase enzymes involved in many manufacturing processes like computer chips, adhesives, and linings of cans and drums. 3.2.3 Catechol 1,2-Dioxygenase Aromatic compounds are usually broken down by microbes like bacteria. Bacterial populations frequently possess genes code for enzymes catechol 1,2-dioxygenase which are able to degrade toxins into catechol and protocatechuate (Nair, Jayachandran, & Shashidhar, 2006). These enzymes are widely distributed among actinobacterial strains. From the result of molecular analysis of catechol-degrading bacteria, the gene catA that codes for C12O is detected between several actinobacterial strains which include Gordonia, Streptomyces, Rhodococcus, Mycobacterium, and Corynebacterium (El Azhari, Devers-Lamrani, Chatagnier, Rouard, & Martin-Laurent, 2010; Hamzah & Al-Bahama, 1994; Harwood & Parales, 1995; Shen et al., 2009). When induced the cultures with benzoic acid, Sutherland et al. (1981) proved activity C12O in four extremely thermophilic strains of

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Streptomyces. At the same time, C12O activity was seen in Rhodococcus sp. NCIM 2891 when the culture medium is induced with phenol (Nadaf, Zanan, & Wakte, 2011). Silva et al. (2012) successfully isolated C12O and C23O enzymes from the actinomycetal strain Gordonia polyisoprenivorans and checked their activity in the range of polluted environment. Immobilized C120 and C230 enzymes showed higher activity which leads to the greater industrial applications. The thermolabile C12O and C23O enzymes from rare actinomycetes genera take part in the breakdown of contaminants from the polluted agricultural environment, which includes aniline and its derivatives (Kaminski, Janke, Prauser, & Fritsche, 1983) but also the degradation of diesel, biodiesel, dibenzothiophene, and chlorinated benzenes (Field & Sierra-Alvarez, 2008; Silva et al., 2012).

3.2.4 Tyrosinase Tyrosinase is a copper-containing enzyme which usually occurs in plant and animal tissues that catalyzes the production of melanin and other pigments by oxidation from the substrate tyrosine, as in the blackening of a peeled or sliced potato exposed to air. As for now, totally three kind of crystal structured tyrosinases have been studied and one among them was isolated from the actinomycete genera, Streptomyces castaneoglobisporus (Toshio, Suzuki, Asano, Matsuzaki, & Nakamura, 1979). These enzymes are omnipresent in nature and provide a huge number of biological functions (Kurane, Suzuki, & Fukuoka, 1984). In plants, tyrosinases are responsible for the browning of open surfaces present in fruits (Muzzarelli, 1985), but in the case of microbes, the defense mechanism of its DNA against reactive oxygen species and radiation by melanin and also binds with the toxic heavy metals (Cambou & Klibanov, 1984; Chakrabarti, Matai, & Chandra, 1978). Biologically active melanin shows loads of advantages like providing UV radiation protection and antitumor activity (Dadachova et al., 2007; Goncalves & PombeiroSponchiado, 2005; Hung, Sava, Hong, & Huang, 2004; Montefiori & Zhou, 1991). In earlier days fungus are utilized as the major source of tyrosinase enzyme (Sambasiva Rao et al., 2012) but now a days actinobacteria are well-known producers of tyrosinases, particularly many Streptomyces species which produce a melanin-like pigment (Kohashi et al., 2004), and due to this, actinobacterial tyrosinases are increasing widespread (Della-Cioppa, Garger, Holtz, McCulloch, & Sverlow, 1998; Della-Cioppa, Garger, Sverlow, 1998; Matoba, Kumagai, Yamamoto, Yoshitsu, & Sugiyama, 2006).

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3.2.5 L-Aminoacid Oxidase L-amino acid oxidases (L-AAO) are the enzymes belong to oxidoreductases that catalyze the oxidative deamination process of L-amino acids to get ketoacids, hydrogen peroxide, and ammonia (Geueke & Hummel, 2002). These enzymes demonstrate broad substrate ranges and are commonly applied for the resolution of racemic mixtures. An L-amino acid oxidase enzyme isolated from rare actinobacteria Rhodococcus opacus DSM 43250 which exhibit a wide range of substrate that includes the amino acids L-phenylalanine, L-alanine, L-lysine, and L-leucine. This enzyme can be able to resolve a racemic mixture of D,L-phenylalanine and D,L-leucine (Geueke & Hummel, 2002). 3.2.6 Putrescine Oxidase Putrescine is a low molecular weight diamine that belongs to the family of compounds termed biogenic amines. Such amines accumulate in foods and putrescine can act as a marker to detect food spoilage caused by Enterobacteriaceae and Clostridium spp. (Santos, 1996; Shalaby, 1996). Putrescine oxidases (PuOs) are the microbial enzyme which catalyze the oxidative deamination of putrescine into 4-aminobutaral, hydrogen peroxide, and ammonia (Agostinelli et al., 2004). Putrescine Oxidases are isolated from numerous actinobacteria, especially from R. erythropolis and Kocuria rosea (Micrococcus rubens) (Adachi, Yamada, & Ogata, 1966; Van Hellemond, Van Dijk, Heuts, Janssen, & Fraaije, 2008). Thin-layer chromatography, ultraperformance liquid chromatography, and gas chromatography are standard analytical methods used to detect biogenic amines (Kolisis & Thomas, 1987; Ray, 1977). Later newer detection methods like biosensors have now been developed. Immobilized putrescine oxidase from actinobacteria K. rosea with multiwalled carbon nanotubes used as a biosensor for the detection of putrescine present in mammalian plasma, with some interference from cadaverine or histamine, and this sensor does not need any prior sample purification (Kunimoto, Aoyagi, Takeuchi, & Umezawa, 1974). 3.2.7 L-Glutamate Oxidases oxidases are strong substrate-specific amino acid oxidases (Costello, Cisar, Kolenbrander, & Gabriel, 1979). The first actinobacterial L-glutamate oxidase was isolated from Streptomyces violascens (Kamei, Asano, Suzuki, Matsuzaki, & Nakamura, 1983). Glutamate oxidases involved a major role in pharmaceutically relevant chiral intermediates L-glutamate

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synthesis especially glutamate to α-ketoglutarate conversion (Patel, 2001a, 2001b). Some of the oxidative enzymes derived from actinobacteria and its applications are listed in Table 2.

3.3 Lignocellulolytic Enzymes From Actinobacteria Lignocellulose is the most plentiful biomass on earth (Isikgor & Becer, 2015). Tons of lignocellulosic wastes are generated significantly by agricultural, forest, and agroindustrial activities annually and they are present in the readily procurable, renewable feedstock, and economically affordable for various lignocelluloses based applications. Lignocellulolytic enzymes are cellulases, hemicellulases, and lignolytic enzymes which play a key role in the processing of lignocelluloses and these are prerequisite for their consumption in various processes. Lignocellulolytic enzymes are the much potent enzymes predominantly produced by actinomycetes which can be widely utilized in various industries based on lignocelluloses (Prakash et al., 2013). Lignocellulases are hydrolytic enzymes which are used to degrade tough lignocelluloses present in the plant biomass including hemicellulases, cellulases, and lignolytic enzymes (Mtui, 2012). Lignin-degrading enzymes have many applications like the recalcitrant lignocellulosic biomass pretreatment for biofuel production, used in various industries like paper industry, textile industry, cosmetic industry, pharmaceutical industries, food industry, wastewater treatment plants, bioremediation processes, and organic synthesis (Abdel-Hamid, Solbiati, & Cann, 2013). Generally actinomycetes the major and attractive groups of lignocellulose producers from which we can get obtain much amount of desired enzymes (Kumar, Biswas, Soalnki, Kumar, & Tarafdar, 2014; McCarthy, 1987; McCarthy & Williams, 1992; Prakash et al., 2013; Vetrovsky, Steffen, & Baldrian, 2014). Celluloses are the components which are used in many industries such as manufacturing of paper and textile fabric industries and major role in the biofuel production from fermentable glucose as inert packing material (Shokri & Adibkia, 2013). Hemicelluloses posses a wide range of applications over various industries and are also used as dietary fiber because of its nontoxicity and biodegradability (Dhingra, Michael, Rajput, & Patil, 2012). Hemicelluloses act as edible coating agent above the packed foods for their stabilization and also used in paper making because of its adhesive properties. In ice-creams and other foods, xyloglucans and β-glucans are used during their stabilizing, gelling, and thickening processes.

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Table 2 Some Oxidative Enzymes From Actinobacteria Enzyme Producers Enzyme Applications

Streptomyces sp. Cholesterol Produces insecticidal proteins oxidase Rhodococcus equi Cholesterol Membrane damage in host, opportunistic infection oxidase in severally immune-suppressed humans (HIV infection) required COX for their infection in host Nocardia

Cholesterol Serum cholesterol measurement oxidase

Rhodochorus erythropolis

Cholesterol Biocatalysis, oxidations of cyclic allylic, bicyclic, oxidase and trycyclic alcohol to synthesize several ergot alkaloids

Streptomyces natalensis

Cholesterol COX-encoding gene (pimE), COX act as a oxidase signaling protein for the biosynthesis of polyene macrolide pimaricin which produce antifungal antibiotic used in food industry; biosynthesis of polyene macrolid pimracin

Streptomyces virginiae

Cholesterol Cloned cholesterol oxidase choL, fragment from oxidase Streptomyces virginiae is used in the oxidation of diosgein to 4-ene-3-keto steroids

Streptomyces lavendulae

Laccase

Biodegradation of xenobiotic compounds, pulp delignication, textile dye bleaching

M. thermophile

Laccase

Fuel industry

S. coelicolor

Laccase

Degradation of dyes used by textile industry

Rhodococcus ruber

Bioremediation

SilA, Streptomyces ipomoea

Lignin degradation

Streptomyces albus

Peroxidase

Biobleaching of kraft pulps

Thermobifida fusca

Peroxidase

Dye industry

Nacardia alba MSA10

Tyrosinase

Food industry, antimicrobial activity, bioremediation of phenol contaminated waters

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Table 2 Some Oxidative Enzymes From Actinobacteria—cont’d Enzyme Producers Enzyme Applications

Streptomyces violascens

Glutamate oxidases

Key role in synthesis of pharmaceutically relevant chiral intermediates

Kocuria rosea

Putrescine oxidase

Used as a biosensor

Hemicelluloses are good source of xylose sugars, which can be easily fermented to form ethanol fuel (G’ırio et al., 2010). For the hydrolysis of hemicellulose, both enzymatic and chemical methods are being used. While in chemical hydrolysis method, there is a use of expensive chemicals, tough conditions, and have some other limitations too. But lignocellulolytic enzymes play a key role in hydrolysis so this method is suitable for industrial applications. Recently utilization of biomass is performed through biorefinery, with significant utilization of all available components and the amount of waste should be less. Hence lignocellulases perform vital functions in biorefinery processes. The genes from numerous lignocellulolytic actinomycetes have been isolated and successfully expressed in different microbes. Gene code for the enzymes GH1 and GH3 from the actinomycetes C. fimi ATCC 484 were cloned in Escherichia coli showed effective hydrolysis of xylanases and celluloses (Gao & Wakarchuk, 2014). Streptomyces reticuli have cel1 gene coding for the enzyme avicelase which has the capacity to hydrolyze crystalline cellulose more efficiently (Schrempf & Walter, 1995). This particular gene was cloned and overexpressed in other microbes like Bacillus subtilis, E. coli, and Streptomyces spp. and owing to the absence of essential regulatory factors, amount of the enzyme was somewhat low (Walter & Schrempf, 1995). The genes xylI and xylII are isolated from xylose-degrading bacteria Actinomadura sp. strain FC7 are cloned and expressed in Streptomyces  thier et al., 1994). From the actinomycetes Streptomyces sp. S27, lividans (E xylanase gene xylBS27 has been cloned and expressed successfully in Pichia pastoris and the cloned product hydrolyzed xylan to xylobiose effectively (Li, Shi, Yang, et al., 2009). Likewise the laccase gene isolated from Streptomyces coelicolor expressed in Streptomyces lividans which produced large amount of laccase with high purity (Dube, Shareck, Hurtubise, Daneault, & Beauregard, 2008). The thermostable laccase gene REN-7 obtained from Streptomyces lavendulae was cloned in E. coli (Suzuki et al., 2003).

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Gene coding for lignin peroxidase get from Streptomyces viridosporus T7A and this gene is cloned into genetically engineered Streptomyces lividans TK64 which showed better lignocellulose degradation than the normal S. lividans TK64 (Wang, Bleakley, Crawford, Hertel, & Rafii, 1990). 3.3.1 Cellulases Cellulases are mainly produced by microorganism like fungi and bacteria that catalyze the breakdown of cellulose materials into simpler monosaccharides. These enzymes are glycosyl hydrolases which are categorized into some families. Cellulases are generally subdivided into four major classes with regard to the mode of action and substrate specificity. These are exoglucanases, endoglucanases, β-glucosidases, and cellobiohydrolases (del-Pulgar & Saadeddin, 2014; Sadhu & Maiti, 2013). These enzymes are specifically important in hydrolyzing crystalline cellulose (delPulgar & Saadeddin, 2014). Among various actinomycetes, Cellulomonas fimi, Streptomyces thermodiastaticus, Thermomonospora curvata, Streptomyces viridosporus and Streptomyces setonii, Microbispora bispora, and Thermobifida fusca are known to be cellulase producers with high yield (Lynd, Weimer, Van Zyl, & Pretorius, 2002; Wilson, 1992). Thermophilic actinomycete Thermobifida fusca is a spore forming actinobacteria reported to produce cellulose-degrading enzyme (Lykidis, Mavromatis, Ivanova, et al., 2007). Cellulomonas fimi produce free cellulases which does not contain cellulosomes (Christopherson et al., 2013). Likewise, Cellulomonas flavigena, a facultative anaerobe, is also reported as a producer of free cellulases that hydrolyze hemicelluloses and celluloses efficiently. The extracellular cellulases are secreted by means of both sec general secretion system and sec independent twin-arginine translocation (TAT) systems. The actinomycetes T. bifida secrete cellulases by utilizing both secretion systems and another actinomycetes S. coelicolor majorly depends on TAT systems for the export of proteins (Lykidis et al., 2007). Various research reports evidently show higher cellulose degradation capacity of actinomycetales than fungal species. 3.3.2 Hemicellulases Xylan, glucuronoxylan, arabinoxylan, mannan, and xyloglucan are the major abundant components of hemicelluloses. Hemicellulases are generally synthesized combined with cellulases enzymes (del-Pulgar & Saadeddin, 2014; Lynd et al., 2002). Earlier studies have specified the production of cellulase free xylanases from Streptomyces roseiscleroticus (Grabski, Forrester,

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Patel, & Jeffries, 1993; Grabski & Jeffries, 1991) and Saccharomonospora viridis (Roberts & Wan, 1998). For the complete hydrolysis of xylan materials, enzymes like endo-1, 4-β-xylanases, α-L-arabinofuranosidases, β-D-xylosidases, acetyl xylan esterases, α-glucuronidases, and ferulic/ coumaric acid esterases are mainly involved. Mannan is hydrolyzed by synergistic action of β-mannosidases, mannanases, and α-galactosidases by means of cleaving β-1,4 linked mannose from nonreducing ends, hydrolyzing β-1,4-glycosidic bonds internally and removing terminal D-galactosyl residues, respectively (Gilbert, 2010). Cellulose hydrolysis is enhanced by the degradation of mannan and xylan was proven by some studies but they are known to inhibit the activity of cellulase (del-Pulgar & Saadeddin, 2014). Many rare strains of actinobacteria show a very good productivity of hemicellulases for example T. bifida and other actinomycetes reported to produce several xylanases like β-1,4-endoxylanases xyl10A, xyl10B, and xil11A, α-L-arabinofuranosidases, xyloglucanases, xylosidases, α-N-arabinofuranosidases xil43, and β-1,3-glucanases GH81 (del-Pulgar & Saadeddin, 2014; Lykidis et al., 2007). Extracellular endo- and exoxylanases such as β-mannanase, xylan binding domain CBM4, xel74, and mannosidase are primarily synthesized by actinomycetes strain Cellulomonas fimi (Christopherson et al., 2013). Extracellular xylanase production has been also detected in Streptomyces aureofaciens (Jeffrey, Norzaimawati, & Rosnah, 2011), Microbispora siamensis (Boondaeng, Tokuyama, & Kitpreechavanich, 2011), and Streptomyces coelicolor when they are grown on agricultural wastes like sugarcane bagasse, orange peel, pomegranate peel, pineapple peels, etc. (Padmavathi, Thiyagarajan, Ahamed, & Palvannan, 2011). Xylanases are the main hemicellulolytic enzyme, which has been majorly produced from Streptomyces sp. 7b (Bajaj & Singh, 2010), Streptomyces sp. CD3 (Sharma & Bajaj, 2005), Thermomonospora fusca (Ball & McCarthy, 1988; McCarthy, Peace, & Broda, 1985), Streptomyces sp. PC22, x SWU10, Streptomyces sp. MDS, and Streptomyces sp. 234P-16I (Thomas, Joseph, Arumugam, & Pandey, 2013). Cellulomonas flavigena ATCC 482 synthesize an unusual mixture of nearly 19 endoxylanases, combined with GH11,GH10, and GH30 xylanases, β-xylosidase GH43, α-glucuronidase, GH51 α-arabinofuranosidase, mannans GH13 and GH26, and β-glucanase GH81 and GH16. Streptomyces flavogriseus showed good productivity of β1,4-glucan glucanohydrolase (Ishaque & Kluepfel, 1980). By using papyrus, rice straw pulp and cotton stalk pulp, Streptomyces chromofuscus, S. albus, and S. rochei have shown the production of xylanase. Then the obtained xylanase used in the study of bleach effects showed improved brightness in the

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presence of EDTA (Nagieb, Milegy, Faat, & Isis, 2014; Rifaat, Nagieb, & Ahmed, 2005). Streptomyces albus and Streptomyces hygroscopicus have shown effective production of biogas by their own xylanases enzymes using oil cake and straw waste as a substrate (Priya, Stalin, & Selvam, 2012). In a study by Ninawe, Lal, and Kuhad (2006), three strains of Streptomyces namely Streptomyces cyaneus, S. caelestis, and S. tendae were found to be excellent producers of xylanolytic enzyme. Tsujibo et al. (2004) demonstrated the production of acetyl xylan esterases and α-L-arabinofuranosidases enzymes from Streptomyces thermoviolaceus OPC-520. Bhosale, Sukalkar, Uzma, and Kadam (2011) estimated production of xylanases as 326 IU/mL from the actinobacteria Streptomyces rameus and sugarcane bagasse combined with peptone and dextrose are act as substrates. When the strain Streptomyces pseudogriseolus was subjected to UV mutagenesis, the xylanase production was improved (Abdel-Aziz, Talkhan, Fadel, AbouZied, & Abdel-Razik, 2011). Thermoactinomyces like Thermomonospora curvata, Thermomonospora alba, and other strains such as Micromonospora, Microbispora bispora, Nocardia, and Saccharomonospora viridis have shown production of acetylesterases, β-xylosidases, and arabinofuranosidases (Ball & McCarthy, 1988). Xylanase production has also been observed in various actinomycetes by various researchers and they are Microtetraspora flexuosa (Berens, Kaspari, & Klemme, 1996), Streptomyces chattanoogensis CECT 3336 (Lo´pez-Ferna´ndez et al., 1998), Streptomyces chattanoogensis UAH 23 (Ferna´ndez et al., 1995), Thermoactinomyces thalophilus (Kohli, Nigam, Singh, & Chaudhary, 2001), Streptomyces violaceoruber (Khurana, Kapoor, Gupta, & Kuhad, 2007), Streptomyces thermocyanaeviolaceus (Shin et al., 2009), Thermomonospora sp. (Ristroph & Humphrey, 1985), and Streptomyces lividans (Herna´ndez-Coronado et al., 1997; Kluepfel, Shareck, Mondou, & Morosoli, 1986; Morosoli, Bertrand, Mondou, Shareck, & Kluepfel, 1986). Hemicellulolytic mannanase enzyme was produced by Microbispora sp. (Jeffrey, 2008), and the other studies have reported the production of β-xylosidases from S. nitrosporeus, Streptomyces albogriseolus, and Micromonospora melanosporea (Van Zyl, 1985). 3.3.3 Lignolytic Enzymes Lignin degradation is done by means of enzyme complex which predominantly contains three enzymes such as laccases, lignin peroxidases, and manganese peroxidases (Mason et al., 2001; Pla´cido & Capareda, 2015). Laccases are the oxidoreductases that indicate the degradation of polyphenol, the major recalcitrant component present in the lignocellulose (Abdel-Hamid et al., 2013; Madhavi & Lele, 2009) and it requires oxygen as a second

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substrate for the enzymatic action. Microbial laccases, or laccase-like enzymes, are increasingly well-known compounds because of its wide industrial applications. Up to 2014, less than 10 actinobacterial laccases belonging to Streptomyces spp. have been fully characterized (Fernandes et al., 2014a). Compared with other bacterial laccases, actinobacterial laccases have more advantages because they possess suitable characteristics which make them fit for industrial applications with increased thermostability, a wide range of pH and stability under denaturing conditions. Laccase is a multicopper blue oxidase that couples the four electron reduction of oxygen with the oxidation of a broad variety of organic substrates, including polyphenols, phenols, anilines, and even certain inorganic compounds (Fernandes, da Silveira, Passos, & Zucchi, 2014b; Fisher & Fong, 2014; Reiss et al., 2011; Ska´lova´ et al., 2009). Typical laccases consist of three domains, where numerous laccases of actinobacterial strains have only two Cu-binding domains, which indicate the structure of the small laccase (SLAC) from Streptomyces coelicolor (Fernandes et al., 2014a, 2014b; Lu et al., 2013; Machczynski et al., 2004). SilA, Ssl1, and SCLAC are some of the two domain laccases isolated from actinobacterial strains Streptomyces ipomoea, Streptomyces sviceus, and Streptomyces sp. C1, respectively (Gunne & Urlacher, 2012; Lu et al., 2013; Molina-Guijarro et al., 2009). Streptomyces griseus, Streptomyces coelicolor, Streptomyces cyaneus, and Thermobifida fusca are some of the producers of small laccases which are either dimers or trimmers (Chen et al., 2013). The enzymes can be used for industries like textile dying, wine cork making, teeth whitening, and many other diagnostic, environmental, and synthetic purposes. Laccases can also be used in bioremediation. Protein ligand docking can be used to anticipate the putative pollutants that can be degraded by actinobacterial laccase. Search for more actinomycetes with high lignolytic yield, using advanced genetic engineering techniques combined with conventional methods. Fernandes et al. (2014a, 2014b) designed specific primers for detection of laccase-like genes in actinomycetes. Arias et al. (2003) have shown laccase production using soya flour by rare actinobacterial strain Streptomyces cyaneus CECT 3335. Veratryl alcohol oxidation and other lignolytic activities have also been described in Streptomyces viridosporus (Ramachandra, Crawford, & Hertel, 1988; Ruttimann, Seelenfreund, & Vicu˜na, 1987). Streptomyces sp. strain EC-22, strain EC1, Streptomyces badius, Streptomyces cyaneus MT813, Thermomonospora chromogena, Thermomonospora fusca, Thermomonospora mesophila, Amncolata autotirophica, and Micromonospora sp. have shown notable activities

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against lignin related compounds (Ball, Betts, & McCarthy, 1989; Godden, Ball, Helvenstein, McCarthy, & Penninckx, 1992).

3.4 Other Industrially Important Actinobacterial Enzymes 3.4.1 Aminoacylase Aminoacylase catalyzes the hydrolysis of acylated D- or L-amino acids to D- or L-amino acids that act on carbon–nitrogen bonds. Aminoacylases play a major role in pharmaceutical industries and this is why the production of this enzyme receives more increasing interest. D-aminoacylases are unusual in microbes, but Szwajcer, Szewczuk, and Mordarski (1981) discovered the occurrence of aminoacylase from the actinobacteria Micrococcus agilis. Many studies have tested the presence of aminoacylase for example 427 strains of Streptomyces and 16 strains of Streptoverticillium were experimented. Among those enzymes, only four strains of streptomycetes like S. roseiscleroticus, S. olivaceus, S. tuirus, and S. sparsogenes were found to be the producers of the enzyme aminoacylase (Sugie & Suzuki, 1980), especially when the medium was supplemented with inducers like D-phenylglycine, D-leucine, D-valine (Sugie & Suzuki, 1978). S. olivaceus and S. tuirus produced D-aminoacylases purified and characterized in accordance with their substrate specificity and both enzymes showed their potential activity at pH 7.0 thus hydrophobic N-acetyl-D-amino acids can be greatly hydrolyzed than the hydrophilic amino acids. Mycobacterium smegmatis and several strains of Streptoverticillium belong to the rare actinomycetes strains which are reported to produce the enzymes penicillin V and L-aminoacylase extracellularly (Matsumo & Nagai, 1972; Oreshina, Penzikova, Levitov, & Bartoshevich, 1982). L-aminoacylase extracted from Streptoverticillium sp. (Borisov et al., 1984) showed a high hydrolytic activity toward aromatic L-amino acids and N-acetylated aliphatic L-aminoacids (Skvortsova, Galeaev, Nys, Svedas, & Savitskaya, 1984). 3.4.2 Protease Proteases catalyze the cleavage of proteins by hydrolyzing peptide bonds and due to this action these are known to be vital for the survival of organisms. Based on the mechanisms utilized for hydrolytic cleavage these proteases can be divided into four different kind of families and those are serine, threonine, cysteine aspartate, and metalloproteinases. Proteases are extensively used in the food, pharmaceutical, detergent, leather, and textile industries (Fan, Zhu, & Dai, 2001; Mozersky, Marmer, & Dale, 2002). Among the extremophilic sources, thermostable proteases have been reported from

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certain haloalkaliphilic bacteria and actinobacteria (Dodia et al., 2008; Thumar & Singh, 2007). The mesophilic actinobacteria have the ability to produce Streptomyces protease pronase 7 M by S. griseus and fradiase 7 M by S. fradiae. Alkaline proteases from the actinobacteria such as S. albidoflavus, S. nigellus, Nocardiopsis, Thermoactinomyces, and Thermomonospora were well characterized (McCarthy et al., 1985). 3.4.3 Chitinase Chitin is a tough, protective, semitransparent polysaccharides and principal components of crustaceans, fungi, and outer coverings of insects. During the enzymatic hydrolysis, chitin can be effectively hydrolyzed by complex of enzymes which contain chitinase and chitobiase. Then the completely deacylated chitin compound is called as chitosane (Muzzarelli, 1985). Chitinolytic complexes generally found in fungi, bacteria, and particularly in actinobacteria. The chitinase have been isolated from the actinomycetes strains like Amycolatopsis (Streptomyces) orientalis (Tominaga & Tsujisaka, 1976), S. griseus (Berger & Reynolds, 1958), S. antibioticus (Jeuniaux, 1966), and several species of Streptomyces spp. (Beyer & Diekman, 1985; Price & Storck, 1975; Tiunova, Prieva, Feniksova, & Kusnetov, 1976). In industrial scale, chitinases are produced in higher amount when the media is supplied with chitin wastes (Muzzarelli, 1985) and isolated and purified chitinases show higher activity at pH 5.0 although more sensitive to temperature. At the same time, Tsujibo et al. (2000) proved that the thermophilic actinomycetes Streptomyces thermoviolaceus OPC-520 actively produces thermophilic chitinases. Same researcher, Tsujibo et al., in the year of 2003 again reported about the alkaliphilic actinomycete, Nocardiopsis prasina that produced chitinase showing activity against fungi Trichoderma sp. The enzyme chitinase from Streptomyces sp. M-20 also exhibits activity against the fungi Botrytis cinerea (Kim, Yang, & Kim, 2003). Streptomyces hygroscopicus produce chitinase enzymes that degrade the chitin present in the stem rot disease producing fungal Sclerotium rolfsii. Thus it can be used along with organic fertilizers to control the stem rot disease (Pattanapipitpaisal & Kamlandharn, 2012). Like these actinobacteria, many chitinase producing novel actinobacterial strains such as Streptomyces aureofaciens CMUAc130 and Streptomyces hygroscopicus (Prapagdee, Kuekulvong, & Mongkolsuk, 2008; Taechowisan & Lumyong, 2003), Streptomyces sp. DA11 (Han, Yang, Zhang, Miao, & Li, 2009), Streptomyces viridificans (Gupta, Saxena, Chaturvedi, & Virdi, 1995), Streptomyces aureofaciens (Taechowisan & Lumyong, 2003), Streptomyces tendae, S. griseus, S. variabilis, S. endus,

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S. violaceusniger (Gherbawy, Elhariry, Altalhi, & El-Deeb, 2012) exhibited effective antifungal activities. 3.4.4 Lipase Lipases, known as triacylglycerol hydrolases, are involved in the digestion and transport of lipids. They are an important group of enzymes which have huge applications in many industries like food, detergent, dairy, and pharmaceutical industries. Actinobacterial lipases play a key role in commercial purposes. Lipases always utilize lipidic carbon, such as fatty acids, glycerols, oils, and tweens as a substrate with organic nitrogen source. From the actinobacterial strain S. lavendulae lipolytic enzyme cholesterol esterase was isolated (Toshio et al., 1979). Rhodococcus (Nocardia) erythropolis is an actinobacteria producing a lipase of the arylesterase group which is able to hydrolyze phthalate esters in to a free phthalic acid and simple n-alcohols (Kurane et al., 1984). These enzymes are active at pH 8.6 and 42°C. The lipase production is also experimented from several Streptomyces strains and reported (Chakrabarti et al., 1978). 3.4.5 Penicillin Amidase Penicillin amidase are biocatalysts able to hydrolyze penicillins. Penicillin acylases are subdivided into three major groups based on their substrate specificity. The penicillin hydrolysis reaction precedes in an alkaline medium and at lower pH values and is reversible. Penicillin amidase production was reported in actinobacteria was seen majorly and trace amount in moulds and yeasts (Hamilton-Miller, 1966; Vandamme & Voets, 1974). Actinobacteria such as Nocardia, Mycobacterium, and Streptomyces are capable to hydrolyze penicillin (Savidge & Cole, 1975; Vandamme, 1980; Vanderhaeghe, 1975). These enzymes are mostly produced intracellularly. They show higher activity in the pH range 7.0 to 8.0.

4. CONCLUSION Actinobacterial enzymes have wide applications in industries and medical fields. In general actinobacterial enzymes are more stable and more active as compared with the enzymes from other organisms. Actinomycetales are unexplored genera which act as a rich resource for oxidative enzymes, lignocellulolytic enzymes, and other industrially important enzymes with potential for biotechnological application. By knowing the genetics and habitats of actinobacteria one can improve the expression system of the

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actinobacterial strains and thus we can improvise easy access. New genetic engineering techniques are now implemented to get a higher yield of novel enzymes from rare actinobacterial strains. The discovery of stable enzymes from extremophilic organisms results in the production of thermophilic, acidophilic, alkaliphilic, and also halophilic enzymes which posses the major utilization in various industries and increased applications in the production of special chemicals, pharmaceutical intermediates, and so on. Sequencing the metagenomes is a recent trend which will clearly give the idea about the rare microorganisms from extreme habitats. From this review we can clearly state that actinomycetes are an essential source of extremozymes, oxidative enzymes, lignocellulolytic enzymes, and other industrially important enzymes. They represent extensive proportion of the aquatic and soil microflora which are responsible for the degradation of biomass present in nature. Numbers of actinomycetes strains are reported as a potential source of novel enzymes. World with a rapid increasing of human population and exhaustion of numerous natural resources, enzyme technology combined with new biotechnological techniques provide good solution to meet many industrial needs and will open up new room of thoughts to the near future.

ACKNOWLEDGMENTS This book chapter was supported by research funds of Pukyong National University in 2015. J.S. grateful to University Grants Commission—Dr. D.S. Kothari Post-Doctoral Fellowship for financial support. Conflict of Interest: The authors declare that they have no conflict of interest.

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