The Role of Actinobacteria in the Production of Industrial Enzymes

Chapter 11

The Role of Actinobacteria in the Production of Industrial Enzymes Richa Salwan and Vivek Sharma CSK-HPKV, Palampur, Himachal Pradesh, India

11.1

INTRODUCTION

The ability of actinobacteria to survive in diverse ecological niches makes them ubiquitous filamentous microbes. They can be found in extreme environmental conditions and are grouped as psychrophilic, thermophilic, alkaliphilic, acidophilic, and halophilic (Shivlata and Satyanarayana, 2015; Ballav et al., 2015). These actinobacteria are the source of various antibiotics (Kandasamy et al., 2012), secondary metabolites (Solecka et al., 2012), and industrial important enzymes (Passari et al., 2015a). The natural ability of actinobacteria to degrade a wide range of substrates (Sambasiva Rao et al., 2012), biotransform organic compounds, and bioconvert agricultural and urban wastes into value added products (Crawford, 1988) is of great economic value. The exploitation of actinomycetes for medical, biotechnological, industrial, and medical purposed is well known and thus offers a strong area of research. Members of actinobacteria are a promising source of a diverse repertoire of enzymes involved in the decomposition of lignocelluloses, lignin, cellulose, and plant residues (Mason et al., 2001; Pasti and Belli, 1985; Watanabe et al., 2003; Scott et al., 2008; Vasanthakumar et al., 2008). Glycoside hydrolases (GH) are known to process complex carbohydrates such as cellulose, chitin, and xylan of plants, representing the most abundant carbon sources. The decomposition of these complex polysaccharides is vital to the global earth carbon cycle and animal nutrition, and is the prime source for several industries, such as biofuel production (Talamantes et al., 2016). Sixty-one GH families, such as cellulases from GH5 and arabinases from GH93, have been identified based on HMM-profile. The domain organization in B40,946 proteins targeting cellulose, xylan, and chitin from bacterial genomes has been done and these proteins are known to have the potential to degrade polysaccharides (Talamantes et al., 2016). The activity of the Streptomyces on CMC and microcrystalline cellulose in combination with putative CAZymes provides evidences of their potential to convert complex substrates into simple sugars. Similarly, Semedo et al. (2000) stated that the potential strain Streptomyces spp. isolated from soil showed significant enzymatic activity. The diverse range of actinobacteria (Das et al., 2006) includes various commercial enzymes viz. α-amylase (Stamford et al., 2001), protease (Dixit and Pant, 2000), cellulase (Techapun et al., 2003), chitinase (Miyashita et al., 1991), keratinase (Mabrouk, 2008), and xylanase (Bode and Huber, 2005; Manivasagan et al., 2013). While a few of them are explored at an industrial scale, the majority of them are still under-harvested. Here in this chapter, we have focused the use of the rich repository of actinobacteria for their ability to secrete enzymes such as amylase, cellulase, protease, xylanase, tyrosinase, lipase, catalase, nd phosphatase, and their exploration for industrial application.

11.2

ENZYMES

Various enzymes of industrial importance have been utilized from various genera of actinobacteria. Other than various metabolites of pharmaceutical interest, actinobacteria produce a number of enzymes, with amylase, proteases, lipase, cellulase, xylanase, inulinase, dextranase, and keratinase having industrial importance (Shivlata and Satyanarayana, 2015; Passari et al., 2015b,2016a). The enzymes responsible for the degradation of complex polysaccharides are often New and Future Developments in Microbial Biotechnology and Bioengineering. DOI: https://doi.org/10.1016/B978-0-444-63994-3.00011-4 © 2018 Elsevier B.V. All rights reserved.

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neglected. Further, the availability of genome and protein sequencing data of actinobacteria has helped in screening these microbes for proteases, cellulases, chitinases, amylases, and xylanases production (Govindharaj et al., 2016). In this chapter, recent reports of various enzymes produced by actinobacteria are reviewed and summarized.

11.3

AMYLASES

Amylases are hydrolases which break down starch molecules into dextrins and smaller polymers of glucose units (Windish and Mhatre, 1965). The starch digestive enzymes are classified into endo and exo types (Pandey et al., 2005). Amylases have pronounced importance in food, fermentation, textile, and paper industries (Pandey et al., 2005). Amylases are found in plants and animals, but microbes are the ideal source for processing starch in industry (Pandey et al., 2005). In particular, the amylases of actinobacteria genus Streptomyces are commonly considered as a potential source of amylolytic enzymes (Vigal et al., 1991). Thermostable amylolytic enzymes have been currently investigated to improve industrial processes of starch degradation. A-amylases belonging to family 13 of the glycoside hydrolase are starch-degrading metalloenzymes, which require Ca21 for activity and stability. These enzymes account for about 30% production with a wide range of applications including bioconversion of starch to sugar syrups, and production of cyclodextrins for the pharmaceutical industry. The enzymatic hydrolysis offers various advantages over acid hydrolysis of starch such as specificity, stability of the generated products, lower energy, and elimination of neutralization steps (Chandrasekaran, 1997). To meet the increasing demand for these enzymes, there is a constant need to identify new enzymes with better properties and cost-effective production techniques. α-amylase enzyme production has been reported from endophytic actinobacteria Nocardiopsis sp. with yam bean (Stamford et al., 2001), whereas Poornima et al. (2008) isolated Actinobacteria sp. AE-19 producing α-amylase from a shrimp pond. In another study, Chakraborty et al. (2009) isolated Streptomyces sp. D1 from the west coast of India that showed α-amylase production. Syed et al. (2009a) reported optimized extracellular α-amylase production from alkali-thermotolerant strain Streptomyces gulbargensis DAS. For detergent based application, haloalkaliphilic Saccharopolyspora sp. strain A9 producing surfactants and oxidant stable, Ca21 ion independent and detergent stable amylase has been explored from the marine ecosystem of India (Chakraborty et al., 2011; Chakraborty et al., 2012; Zhao et al., 2016).

11.4

LIGNOCELLULOLYTIC ENZYMES

Lignocellulose, a main constituent of plant matter, is composed of lignin, cellulose, and hemicellulose (Limayem and Ricke, 2012), and is the most abundant renewable biomass on earth (Isikgor and Becer, 2015). The hydrolysis of lignocellulose is accompanied by hydrolytic enzymes, which include cellulases, hemicellulases, and lignolytic enzymes. The cellulolytic enzymes are utilized for biofuel production, textiles, pulp and paper, detergents, food, and feed industries. Similarly, hemicellulases have importance in bio-bleaching, saccharification of polysaccharides, waste paper deinking, clarification of fruit juices, Eefibres, and fodder (Soni and Kango, 2013). Hemicellulolytic microbes are key players in recycling hemicelluloses. Xylanases (EC 3.2.1.8) cleave the xylan, a major constituent of hemicellulose. The enzymes acting on this substrate could improve the economics of processing lignocellulosic materials for various industrial applications. The use of cellulase-free xylanases has received great attention in the development of environmentally friendly technologies in the paper and pulp industry. The lignin-degrading enzymes having various application in biofuel production, paper and pulp, textiles, food, bioremediation, and pharmaceutical industries (Abdel-Hamid et al., 2013). Among microbes, actinomycetes are an attractive source of hemicellulases which is composed of xylan and mannan units (Lynd et al., 2002; del-Pulgar and Saadeddin, 2014). The complete breakdown of xylan is mediated by a combined action of α-L-arabinofuranosidases, endo-β-1,4-xylanases, α-glucuronidases, β-D-xylosidases, ferulic acid esterases, and acetyl xylan esterases. Mannan, another component of hemicelluloses, is hydrolyzed by mannanases (EC 3.2.1.78), β-mannosidases (EC 3.2.1.25), and α-galactosidases (EC 3.2.1.22) (Adav et al., 2010; del-Pulgar and Saadeddin, 2014). The mannanases hydrolyze β-1, 4-glycosidic bonds into oligomers whereas β-mannosidase hydrolyze nonreducing ends of β-1, 4 linked mannose and α-galactosidase break down D-galactosyl residues connected by α-1, 6 bonding (Gilbert, 2010).

11.4.1

Lignolytic Enzymes

The hydrolysis of lignin is catalyzed by laccases (EC 1.10.3.2), manganese peroxidases (EC 1.11.1.13), and lignin peroxidases (EC 1.11.1.14) (Miyazaki, 2005; Hilde´n et al., 2009). Laccases constitute a class of oxidoreductases that degrades polyphenol, a major recalcitrant component of lignocellulose (Claus, 2003; Couto, and Toca-Herrera, 2007). Laccases of benzenediol:oxygen oxidoreductases EC 1.10.3.2 are blue multicopper oxidases, and active over a wide

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range of aromatic and nonaromatic compounds (Claus, 2004). These were first discovered in plants, followed by fungi, and hundred years later in bacteria (Alves et al., 2014). Presently, most studies on laccases are focused on fungi due to the physiological roles of their potential for industrial application or their biochemical properties, with very few studies on bacteria (Piscitelli et al., 2010; Alves et al., 2014). Laccases have low substrate specificity, which helps in degrading complex compounds by making use of manganese and lignin peroxidases. Lignin peroxidases oxidize phenolic and nonphenolic aromatic rings that form B90% content of lignin. Laccases or Laccase-like multicopper oxidases contain four Cu atoms (Couto and Herrera, 2006; Niladevi and Prema, 2008), whereas in actinomycetes, only two Cu-binding domains have been detected (Harkin and Obst, 1993; Ruiz-Duen˜as and Martı´nez, 2009), including small laccase-like multi copper oxidase (Niladevi and Prema, 2008; Ruiz-Duen˜as and Martı´nez, 2009) and long laccase-like multi copper oxidase (LMCO). Actinobacteria are considered of great importance in the degradation of recalcitrant and relatively complex polymers naturally found in litter and soil such as lignin and humic acid (Goodfellow and Williams, 1983; Godden et al., 1992; Lee 1997; Bugg et al., 2011). In particular, the order Actinomycetales has attracted industrial attention due to its outstanding capacity to produce compounds with high biotechnological values. Studies have been reported on LMCO characterization from S. cyaneus CECT 3335 (Arias et al., 2003), S. lavendulae REN-7 (Suzuki et al., 2003), S. griseus IFO 13350 (Endo et al., 2003), S. coelicolor M145 (Machczynski et al., 2004), S. ipomoea CECT 3341 (Molina-Guijarro et al., 2009), S. psammoticus MTCC 7334 (Niladevi et al., 2008), and other Streptomyces spp. (Gunne and Urlacher, 2012; Lu et al., 2013; Alves et al., 2014). Alves et al. (2014) reported that 10 laccase enzymes with huge industrial importance have been characterized from Streptomyces that provide the basis for a distinct family and two-domain laccases. Laccases have been reported as dimmers and trimmers in various species of the genus Streptomyces and Thermobifida fusca (Gunne and Urlacher, 2012). The LMCO find their applications in diverse industrial processes including textiles, cleansing products for cloth washing, food for removing of unwanted phenolic compounds in bread, juices, beer and wine, removal of oxygen in packed food, pulp and paper for cellulose bleaching, cross-linking in ligninaceous compounds, deinking of printed paper and pharmaceuticals such as anesthetics, antibiotics, and anti-inflammatory biosensors in immunoassays, as well as in nanobiotechnology, cosmetics, and bioremediation (Couto and Herrera, 2006; Kunamneni et al., 2008; Widsten and Kandelbauer, 2008; Shraddha et al., 2011; Alves et al., 2014).

11.4.2

Xylanases

Xylan is formed by substitutions of D-xylosyl residues and arabinosyl, acetyl, and glucuronosyl units (Thomson, 1993; Tomme et al., 1995; Cazemier et al., 1999). The breakdown of xylan is an important step for its proper utilization in nature. Xylanases are classified into GH families 5, 7, 8, 10, 11, and 43, which hydrolyze β-1,4-glycosidic bonds internally, and β-D-xylosidases belonging to GH families 3, 39, 43, 52, and 54 that cleave the xylose monomers from nonreducing ends of oligosaccharides (Henrissat, 1991). Xylanases are found in a variety of organisms and the genes encoding them have been cloned in homologous and heterologous hosts for over-expression with altered biochemical properties for commercial applications. The presence of distinct catalytic and cellulose-binding domains with a separate noncatalytic domains have revealed regions conferring enhanced thermo-stability to certain xylanases. The tyrosine and tryptophan amino acids in the substrate binding site and glutamate and aspartate residues in the catalytic mechanism have been revealed (Saini et al., 2015). Various studies have been reported for xylanases production from various species of actinomycetes. T. bifida has been reported for the production of β-1, 4-endoxylanases, xylosidases, β-1,3-glucanases, xyloglucanases, α-N-arabinofuranosidases, and α-L-arabinofuranosidases (del-Pulgar and Saadeddin, 2014). In similar studies, the production of endo- and exo-xylanases, β-mannanase, mannosidase, and xel74 has been reported from Cellulomonas fimi (del-Pulgar and Saadeddin, 2014; Christophersonet al., 2013). Cellulomonas flavigena ATCC 482 has been reported for production of xylanases belonging to family GH10, GH11, GH13, GH16, GH26, GH30, GH43, GH51, and GH81 (Christopherson et al., 2013). Similarly, reports are available on Streptomyces flavogriseus for the production of β-1,4-glucan glucanohydrolase and on Streptomyces sp. SirexAA-E for β-mannosidase, β-xylanase, β-xylanase, and acetylxylan esterase (Takasuka et al., 2013). Actinobacteria are a potential source of primary and secondary metabolites but less attention has been paid to xylanases (Mansour et al., 2003; Kansoh and Nagieb, 2004; Rawashdeh et al., 2005; Passari et al., 2017). The advantage associated with xylan degradation by actinobacteria over fungi is the lack of cosecretion of cellulases (Chen et al., 1997; Christov et al., 1999; Ninawe et al., 2006; Passari et al., 2016a). Actinobacterial xylanases have several advantages such as high thermostability, noncellulytic activity, and broad pH range activity required for various industrial applications (Niehaus et al., 1999; Georis et al., 2000). Such cellulase-free xylanases with alkaliphilic and high

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temperature active properties have been reported from Thermoactinomyces thalophilus (Kohilu et al., 2001), Actinomadura sp. (Sriyapai et al., 2011), and from other species (Bode and Huber, 2005; Manivasagan et al., 2013). In India, xylanases from actinomycetes have been characterized from soil samples (Ninawe et al., 2006) and the National Aluminum Company Limited, Orissa (Krishna et al., 2008).

11.4.3

Cellulases

Cellulose, the most abundant organic source (Spano et al., 1975), consists of glucose units linked by β-1,4-glycosidic bonds in a linear mode. Hemicellulases enhance cellulose hydrolysis by the cooperative action of mannanases and xylanases belonging to glycosyltransferases. The difference in the type of bond and crystalline form make cellulose more resistant to digest and hydrolyze. The enzymes required for the hydrolysis of cellulose include endoglucanases, exoglucanases, and β-glucosidases (Matsui et al., 2000). In the current industrial processes, cellulolytic enzymes have important applications in the production of biofuels from lignocellulosic biomass, in the color extractions of juices, detergents causing color brightening and softening, biostoning of jeans, pretreatment of biomass that contains cellulose to improve nutritional quality of forage, and pretreatment of industrial wastes (Buchert et al., 1997; Niehaus et al., 1999; Nakamura et al., 2001). Cellulose is one of the most abundant and renewable natural biological resources, and the cost of enzyme production can be significantly reduced by using low value biological substrates (Kumar et al., 2012). In anaerobes, a large complex of cellulases and other glycosyl hydrolases known as cellulosomes are involved in the hydrolysis of cellulose. Contradictory to this, aerobic actinobacteria utilizes enzymes containing carbohydrate binding domains. A large number of genomes sequencing projects have led to the identification of several putative cellulose-degrading enzymes belonging to families GH5, GH6, GH8, GH9, GH12, GH48, and GH51 in the genomes of the actinobacteria. Among 11 organisms tested for cellulose degradation, the 3 bacteria with the highest cellulase activity Actinosynnema mirum, Cellulomonas flavigena, and Xylanimonas cellulosilytica, have been identified. The genome sequence data identified several actinobacteria that were not previously known to degrade cellulose as cellulolytic organisms (Anderson et al., 2012). The alkali-tolerant cellulase is primarily reported from Streptomyces and Thermoactinomyces (Techapun et al., 2003). The cellulase production from the Streptomyces drozdowiczii strain of Brazilian forest soil has been reported using agro-industrial products and also evaluated for its application in the textile and detergent industries (Grigorevski de Lima et al., 2005). In a separate study, 35 strains of actinobacteria from the guts of finfish were evaluated for cellulase activity (Murugan et al., 2007). The cellulase production from Streptomyces malaysiensis was studied using submerged fermentation technique with a combination of brewer’s spent grain and wheat bran as carbon source supplemented with corn steep liquor as nitrogen source (Nascimento et al., 2009). From India, Streptomyces noboritoensis strain isolated from Southwest ghats of Tamil nadu was studied for cellulase production (Arunachalam et al., 2010). Streptomyces viridobrunneus actinomycete strain has been reported as a promising cellulolytic strain for its ability to produce cellulases from agro-industrial residues in Brazil (da Vinha et al., 2011).

11.4.4

Chitinases

Chitin is one of the most widely distributed carbohydrates after cellulose and is a component of fungal cell walls and exoskeletons and the eggshells of insects (Metcalfe et al., 2002). Chitinases are produced by many microbes such as actinobacteria, higher plants, and animals, and play important physiological and ecological roles (Gooday, 1990). The chitinases production is correlated to antifungal property (Kunz et al., 1992; Mathivanan et al., 1998) and the recycling of chitinous wastes from shrimp shells and chitin from the seafood industry (Mukherjee and Sen, 2004). Addition of chitin to soil has been shown to increase counts of actinobacteria including Streptomycetes, and chitin amendment has been used as a biocontrol measure in soil. Chitinases cleave the β-1,4 linkages in chitin into oligomeric units which are further hydrolyzed by N-acetylglucosaminidases into GlcNAc monomer (Tsujibo et al., 2003). Chitinases are classified based on their amino acid sequences, structural properties and mechanistic features into subfamilies 18 and 19 of the glycosyl hydrolases (Metcalfe et al., 2002). The genus Streptomyces of actinobacteria is widely studied for chitinases (Miyashita et al., 1991). A number of actinobacteria, Nocardiopsis prasina, Streptomyces sp. M-20, Streptomyces coelicolor A3, and Streptomyces aureofaciens CMUAc130, have been explored for chitinases production (Ralph Berger and Reynold, 1958; Price and Storck, 1975; Tiunova et al., 1976; Beyer and Diekmann, 1985; Tsujibo et al., 2000; Metcalfe et al., 2002; Kim et al., 2003; Tsujibo et al., 2003; Taechowisan et al., 2003; Xiao et al., 2005). Besides this, four strains of actinobacteria, Streptomyces

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griseoloalbus JCM4480, Streptomyces clauifer JCM5059, Streptomyces anulatus NBRC13369, and S. griseus subsp., produced chitinase unique compounds, showing selective inhibition of the insect GlcNAcase (Usuki et al., 2006). Prapagdee et al. (2008) isolated Streptomyces hygroscopicus with chitinase activity against phytopathogenic fungi.

11.4.5

Proteases

Proteases constituting B60% of the total enzyme market with potential for diverse industrial importance including detergents, food, dehairing, baking and brewing, silver recovery from photographic film, and bioremediation (Germano et al., 2003). Additionally, alkaline proteases used in leather, textile, organic synthesis, and waste water treatment have been characterized from a wide range of organisms including actinobacterian (Kalisz, 1988; Kumar and Takagi, 1999). The extracellular proteases from Streptomyces nogalator strain Ac 80 (Mitra and Chakrabartty, 2005), thermophilic proteases of Streptomyces sp. (De Azeredo et al., 2004) from Brazilian cerrado soil, alkaliphilic acinomycete (Mehta et al., 2006), S. gulbargensis DAS 131 (Dastager et al., 2008), marine actinobacteria (Ramesh et al., 2009), and flesh content of the Mud crab, Scylla serrate (Karthik et al., 2010), soil samples of the Northern Himalayas (Balachandran et al., 2012), have been explored for protease production (Manivasagan et al., 2013). Serine proteases produced by Streptomyces lactamdurans (Ginther, 1978) and Streptomyces peucetus (Gibb and Strohl, 1988) are reported to coordinately regulate the cellular protein turnover associated with secondary metabolism and morphogenesis (Suzuki et al., 1997). Proteases from mesophilic (Moormann et al., 1993; Boeckle et al., 1995) and thermophillic actinomycetes have been characterized (Mohamedin, 1999). Another alkaline protease from Nocardiopsis sp. NCIM 5124 has been characterized (Dixit and Pant, 2000). The hydrolysis of keratin-containing wastes using potential microbes offers an attractive, efficient, and alternate method for recycling keratin wastes from waste water treatment, textile, medicine, cosmetic, leather, feed, and poultry processing industries as well as the leather industry (Mukhopadhyay and Chandra, 1990; Mukhopadhyay and Chandra, 1993; Bertsch and Coello, 2005; Tatineni et al., 2008; Syed et al., 2009b). A number of actinobacteria such as Streptomyces sp. from Egypt (Mabrouk, 2008), Streptomyces albus AZA (Esawy, 2007), Streptomyces strain BA7 from Turkey (Korkmaz et al., 2003), and Streptomyces pactum DSM 40530 (Boeckle et al., 1995) have been studied for keratinase production (Al-Zarban et al., 2002). Moreover, various researchers reported that different types of Streptomyces species, mainly S. pactum, S. albus, S. fradiae, S. thermoviolaceus, and S. treptomyces sclerotialus were found to be positive for keratinase production (Boeckle et al., 1995; Chitte et al., 1999; Al-Sane et al., 2002; Chao et al., 2007; Yadav et al., 2011; Shata and Farid, 2012). The endophytic Micromonospora strains from the Egyptian herbal plant were also reported for keratinolytic activity (Ahmed et al., 2010; Manivasagan et al., 2013).

11.4.6

Lipase Enzyme

Lipases have the ability to break carboxylic ester bonds in fats to form diglycerides, monoglycerides, fatty acids, and glycerol. The importance of lipases for different applications has been growing rapidly. Biocatalyst thermostability allows a higher operation temperature, which is clearly advantageous because of higher stability and process yield.

11.5 ENZYMES USED FOR BIOTRANSFORMATION/MODIFICATION OF NATURAL PRODUCTS 11.5.1

Prenyltransferase

Phenazines are a class of over 150 nitrogen-containing aromatic compounds of bacterial and archeal origin having broad antibiotics-specificity and other biological functions. Several prenyltransferases from actinobacteria have been reported to catalyze C-prenylation of phenazines into important bioactive molecules. Streptomyces sp. CNQ-509 can serve as a promising candidate for biocatalytic applications as several prenyltransferases have been reported from the genome sequence (Leipoldt et al., 2015). In another study, the membrane-bound prenyltransferase-encoding gene cnqPT1 involved in O-prenylation of a phenazine scaffold has been reported from Streptomyces sp. A new class of phenazine prenyltransferase including membrane bound 1,6-dihydroxyphenazine prenyltransferase Mpz10 has been reported from a marine sponge-associated Streptomycete (Zeyhle et al., 2014a; Zeyhle et al., 2014b), which is a promising candidate for such bioactive compounds (Zeyhle et al., 2014a; Zeyhle et al., 2014b; Zhao et al., 2016) (Fig. 11.1).

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FIGURE 11.1 Applications of actinobacteria in different industries.

11.5.2

Halogenase

Halogenases are responsible for halogenation of various natural products, where chlorination is the most common modification, followed by bromination (Neumann et al., 2008). A SAM-dependent chlorinase SalL involved in the biosynthesis of salinosporamide A has been reported from marine actinobacteria Salinispora tropica (Eustaquio et al., 2008). The flavin-dependent halogenases are of particular interest due to their functions in the introduction of chloride and bromide into natural products. Fluorinated natural products are rare in nature, and it is thus of great interest to identify a fluorinase gene in Streptomyces xinghaiensis. The fluorinase was proved to be involved in the biosynthesis of fluoroacetate by in vivo study, and S. xinghaiensis is therefore the first microorganism to produce fluorometabolite (Huang et al., 2014). It will be interesting to test more halogenases for biosynthesis of natural active products (Zhao et al., 2016) (Fig. 11.2).

11.6 11.6.1

OTHER INDUSTRIAL APPLICATIONS OF ACTINOMYCETES Food Industry

Microbial proteases have been exploited in the food industry for preparing hydrolysates of protein of high nutritional value, blood pressure regulation, infant food formulations, therapeutic dietary products, and fruit juice fortification. Alkaline proteases are used for protein hydrolysate production from natural protein substrates.

11.6.2

Leather Industry

The treatment of leather using enzymatic approaches offers several advantages, being ecofriendly, easy to control, and reduced waste over conventional methods involving chemicals such as hydrogen sulfide, etc., which create environmental pollution. Alkaline proteases having elastolytic and keratinase activity are of potential for use in leather-processing industries for soaking, dehairing, and bating of preparing hides. The treatment with enzymes also destroys undesirable

The Role of Actinobacteria in the Production of Industrial Enzymes Chapter | 11

O H H O H

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H H H

H H H H

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Endophenazine A

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FIGURE 11.2 Overview of conversion of phenazines to their bioactive dertivatives by prenyltransferase system of actinobacteria.

pigments, therefore clean hide can be recovered. Isolate Actinomadura keratinilytica strain cpt29 and strain Nocardiopsis sp. produce thermostable and alkaline active enzyme with application in the leather industry.

11.6.3

Detergent Industry

Enzymes are important candidates for the detergent industry in efficiently removing proteinaceous strains in comparison to conventional detergents. Strain Saccharomonospora viridis SJ-21 and strain Nocardiopsis sp. produce thermostable and alkaline active protease with application in laundry for the washing of textiles).

11.6.4

Photographic Industry

Actinobacteria with the ability to produce proteases are used in the bio-processing of used X-ray or photographic films for silver recovery. Various species of alkalitolerant and alkaliphilic actinobacteria produce alkaline stable proteases and keratinase of commercial importance. These proteases are employed in the process of silver recovery from used X-ray or photographic film that limits undesirable environmental pollution caused by burning. Proteolytic hydrolysis not only extracts silver but also helps in recycling polyester films.

11.6.5

Pharmaceutical and Medical Applications

Actinomycetes produce a variety of antibiotics and secondary metabolites that have antifungal, anti-tumor, and immunosuppressive activities. Thermostable keratinases from Saccharomonospora viridis SJ-21 and Thermomonospora curvata have been reported for pharmaceutical applications.

11.6.6

Silk Degumming

Different strains of actinomycetes have the capacity to degum silk fibers by producing thermostable and alkalin tolerant proteases (More et al., 2013). Only a few patents have been filed describing the use of proteases for the degumming of

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silk. The degumming process is generally expensive and therefore alternative methods such as protease enzyme preparations are in demand for degumming the silk prior to dyeing.

11.6.7

Bioremediation

Actinomycetes serve as attractive candidates for deducting pollutants from the environmental soils contaminated with organic pollutants. Actinomycetes have the capability to degrade petroleum hydrocarbons (Sharma, 2014). The genus Streptomyces plays an important role in the degradation of hydrocarbons (Radwan et al., 1998; Barabas et al., 2001).

11.7

CONCLUSION AND FUTURE PROSPECTS

Bioprospecting actinobacteria represents an extensive pool of industrial and pharmaceutically relevant biomolecules, such as cellulose, lignin, starches, hemicelluloses, and chitin, for efficient degradation. Such enzymatic activity can be explored keeping in view their efficiency, cost effectiveness, and environmentally friendly contribution to meeting industrial demands throughout the world. Further, the vast range of genes responsible for the hydrolysis of polysaccharides in the genome of actinobacteria suggests the potential of these microbes for industrial applications. Therefore, continuous studies on identification and characterization of potential genes and their encoding enzymes targeting different industrial applications are required for the development of sustainable and cost-effective production for commercialization. Their high abundance and metabolic versatility also provide a new robust gateway to bioremediation of pollutants and organic residues.

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FURTHER READING Adams, A.S., Jordan, M.S., Adams, S.M., Suen, G., Goodwin, L., Davenport, K.W., et al., 2011. Cellulose-degrading bacteria associated with the invasive woodwasp Sirex noctilio. ISME J. 5 (8), 1323 1331. Anitha, A., Rebeeth, M., 2009. In vitro antifungal activity of Streptomyces griseus against phytopathogenic fungi of tomato field. AJPS 2 (2), 119 123. El-Bondkly, A.M., El-Gendy, M.M., 2010. Keratinolytic activity from new recombinant fusant AYA2000, derived from endophytic Micromonospora strains. Can. J. Microbiol. 56 (9), 748 760. Renu, S., Kapoor, V., Kumar, V., 2012. Utilization of agro-industrial wastes for the simultaneous production of amylase and xylanase by thermophilic actinomycetes. Braz. J. Microbiol. 43 (4), 1545 1552. Taylor, C.R., Hardiman, E.M., Ahmad, M., Sainsbury, P.D., Norris, P.R., Bugg, T.D.H., 2012. Isolation of Bacterial Strains able to metabolize lignin from screening of environmental samples. J. Appl. Microbiol. 113, 521 530. Williams, C., Lee, C., Garlich, J., Shih, J.C.H., 1991. Evaluation of a bacterial feather fermentation product, feather-lysate, as a feed protein. Poult. Sci. 70 (1), 85 94. Williams, P.G., Buchanan, G.O., Feling, R.H., Kauffman, C.A., Jensen, P.R., Fenical, W., 2005. New cytotoxic salinosporamides from the marine Actinomycete Salinispora tropica. J. Org. Chem. 70, 6196 6203.