- Email: [email protected]
Process strategies for production of xylanase in submerged culture by Melanocarpus albomyces IITD3A
Abstracts / Journal of Biotechnology 136S (2008) S290–S344
S301
References
V1-Y-114
Haltrich, D., Laussamayre, B., Steiner, W., 1994. Xylanase formation by Sclertium rolfsii: effect of growth substrates and development of a culture medium using statistically designed experiments. Appl. Microbiol. Biotechnol. 42, 522–530. Jiang, Z.Q., Yang, S.Q., Yan, Q.J., Li, L.T., Tan, S.S., 2005. Optimizating xylanase production by a newly isolated strain CAU44 of the thermophile Thermomyces lanuginosus 2 863–867. Luciana, A.O., Ana, L.F.P., Elias, B.T., 2006. Production of xylanase and protease by Penicillium janthinellum CRC 87M-115 from different agricultural wastes. Bioresour. Technol. 97, 862–867.
Study of some proteolytic enzymes of submerge cultivated higher basidiomycetes
doi:10.1016/j.jbiotec.2008.07.1882
Eugenia Tozik 1,∗ , Tatyana Dmitriyeva 1 , Nina Denisova 2 , Nikolay Petrischev 3 , Mark Shamtsyan 1 1
St. Petersburg State Institute of Technology (Technical University), Moscovsky prospect, 26, St. Petersburg 190000, Russia 2 V.L. Komarov Botanical Institute of Russian Academy of Sciences, Prof. Popov str., 2, St. Petersburg 197376, Russia 3 I.P. Pavlov State Medical University, Leo Tolstoy str. 6/8, 197022, St. Petersburg, Russia
V1-Y-079
E-mail address: [email protected] (M. Shamtsyan).
Process strategies for production of xylanase in submerged culture by Melanocarpus albomyces IITD3A
The fungus, Melanocarpus albomyces IIS 68, produces xylanase (160 IU ml−1 ) along with xylan-debranching enzymes (Saraswat and Bisaria, 1997). For isolating high xylanase producing mutants, sporulation of the fungus was induced. The mutant obtained after EMS treatment, M. albomyces IITD3A, was stable and produced high xylanase activity (310 IU ml−1 ) after 72 h at pH 6.0 and 70 ◦ C on wheat straw. However, when the mutant was cultivated on an inexpensive soluble carbon source obtained by alkaline extraction of wheat straw, it produced 415 IU ml−1 in 36 h. The statistical optimization of the production medium revealed that xylanase activity was sensitive to pH. Therefore, when pH of the production medium in 14 l bioreactor was controlled on-line at pH 7.8, the maximum activity obtained was 415 IU ml−1 after 36 h. On cycling the pH between 7.8 and 8.2, the maximum xylanase activity obtained was 415 IU ml−1 after 24 h. Hence, the productivity increased from 11,528 to 16,670 IU l−1 h−1 . The fungal morphology changed from dispersed filaments at 400 rpm to small pellets of size 1–2 mm at 600 rpm and resulted in xylanase activity of 480 IU ml−1 in 24 h compared to 415 IU ml−1 at 400 rpm. Hence, the change in morphology of the fungal biomass seems to have contributed to the improved activity at 600 rpm. Further, on optimising aeration rate to 0.25 vvm, the maximum xylanase activity of 541 IU ml−1 was attained after 25 h. The overall volumetric productivity of xylanase by the mutant was thus enhanced to 21,640 IU l−1 h−1 , resulting in six-fold enhancement over the wild type. The translation of the results to 150 l bioreactor on the basis of same impeller tip speed resulted in 450 IU ml−1 activity in 24 h.
Mushrooms can synthesize diverse biologically active substances. Biologically active and valuable chemical substances can be obtained both, as independent end products of mycelium cultivation, as well as by-products, for example, of the industrial production of food or stern biomass. Our studies were devoted to the search of some proteolytic enzymes produced by higher basidiomycetes during submerge cultivation, namely milk-clotting, fibrinolytic and thrombolytic enzymes. With the production of cheeses the key feature for the successful decision of technological process is the selection of the milk-clotting enzyme. The rennet (rennin, chymosin), produced in the abonasum (division of stomach) of young ruminant animals, was used by millennia in the cheese making for milk coagulation. The replacement of the expensive rennet by microbial proteases of specific action is economically advantageous, promising and is always urgent Requirements for the substitutes of the rennet are strict and specific—their enzymatic properties must maximally approach those of accepted as the standard natural rennin, i.e. together with the high milk-clotting activity they must possess the insignificant general proteolytic activity, which leads to the unspecific proteolysis of the proteins of casein. Milk-clotting enzymes were purified and characterized from the native liquids of several mushrooms. Lyophilized active fractions possess the high levels of milk-clotting activity. Enzymes have molecular weight of 37–41 kDa, temperature optimum 34–37 ◦ C, the optimum of pH 6.4–6.5. The use of this enzyme preparations as the milk-clotting agent led to the formation of dense milk clusters without the aftertaste of bitterness. It was very interesting to found, that the same fractions of native liquid which was actively clotting milk, possess significant fibrinolytic activity. In vivo experiments on Wistar male rats also demonstrates the ability of the purified preparations injected intravenously, efficiently to solve the thrombus in venues and arteries of experimental animals.
Reference
doi:10.1016/j.jbiotec.2008.07.1884
Saraswat, V., Bisaria, V.S., 1997. Biosynthesis of xylanolytic and xylan debranching enzymes in Melanocarpus albomyces IIS 68. J. Ferment. Bioeng. 83, 352–357.
V1-P-002
doi:10.1016/j.jbiotec.2008.07.1883
Exopolysaccharide production in batch and semi-continuous fermentation of Cordyceps sinensis
Ranjita Biswas ∗ , Vikram Sahai, Saroj Mishra, Virendra S. Bisaria Department of Biochemical Engineering & Biotechnology, Indian Institute of Technology Delhi, New Delhi, India
Yuan-Shuai Liu ∗ , Po-Hong Leung, Jian-Yong Wu Department of Applied Biology & Chemical Technology, the Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong E-mail address: [email protected] (Y.-S. Liu). Cordyceps sinensis (Berk.) Sacc., known as DongChongXiaCao in Chinese, is a precious medicinal fungus. Polysaccharides (PS) represent a major class of the bioactive compounds of Cordyceps and
S301
References
V1-Y-114
Haltrich, D., Laussamayre, B., Steiner, W., 1994. Xylanase formation by Sclertium rolfsii: effect of growth substrates and development of a culture medium using statistically designed experiments. Appl. Microbiol. Biotechnol. 42, 522–530. Jiang, Z.Q., Yang, S.Q., Yan, Q.J., Li, L.T., Tan, S.S., 2005. Optimizating xylanase production by a newly isolated strain CAU44 of the thermophile Thermomyces lanuginosus 2 863–867. Luciana, A.O., Ana, L.F.P., Elias, B.T., 2006. Production of xylanase and protease by Penicillium janthinellum CRC 87M-115 from different agricultural wastes. Bioresour. Technol. 97, 862–867.
Study of some proteolytic enzymes of submerge cultivated higher basidiomycetes
doi:10.1016/j.jbiotec.2008.07.1882
Eugenia Tozik 1,∗ , Tatyana Dmitriyeva 1 , Nina Denisova 2 , Nikolay Petrischev 3 , Mark Shamtsyan 1 1
St. Petersburg State Institute of Technology (Technical University), Moscovsky prospect, 26, St. Petersburg 190000, Russia 2 V.L. Komarov Botanical Institute of Russian Academy of Sciences, Prof. Popov str., 2, St. Petersburg 197376, Russia 3 I.P. Pavlov State Medical University, Leo Tolstoy str. 6/8, 197022, St. Petersburg, Russia
V1-Y-079
E-mail address: [email protected] (M. Shamtsyan).
Process strategies for production of xylanase in submerged culture by Melanocarpus albomyces IITD3A
The fungus, Melanocarpus albomyces IIS 68, produces xylanase (160 IU ml−1 ) along with xylan-debranching enzymes (Saraswat and Bisaria, 1997). For isolating high xylanase producing mutants, sporulation of the fungus was induced. The mutant obtained after EMS treatment, M. albomyces IITD3A, was stable and produced high xylanase activity (310 IU ml−1 ) after 72 h at pH 6.0 and 70 ◦ C on wheat straw. However, when the mutant was cultivated on an inexpensive soluble carbon source obtained by alkaline extraction of wheat straw, it produced 415 IU ml−1 in 36 h. The statistical optimization of the production medium revealed that xylanase activity was sensitive to pH. Therefore, when pH of the production medium in 14 l bioreactor was controlled on-line at pH 7.8, the maximum activity obtained was 415 IU ml−1 after 36 h. On cycling the pH between 7.8 and 8.2, the maximum xylanase activity obtained was 415 IU ml−1 after 24 h. Hence, the productivity increased from 11,528 to 16,670 IU l−1 h−1 . The fungal morphology changed from dispersed filaments at 400 rpm to small pellets of size 1–2 mm at 600 rpm and resulted in xylanase activity of 480 IU ml−1 in 24 h compared to 415 IU ml−1 at 400 rpm. Hence, the change in morphology of the fungal biomass seems to have contributed to the improved activity at 600 rpm. Further, on optimising aeration rate to 0.25 vvm, the maximum xylanase activity of 541 IU ml−1 was attained after 25 h. The overall volumetric productivity of xylanase by the mutant was thus enhanced to 21,640 IU l−1 h−1 , resulting in six-fold enhancement over the wild type. The translation of the results to 150 l bioreactor on the basis of same impeller tip speed resulted in 450 IU ml−1 activity in 24 h.
Mushrooms can synthesize diverse biologically active substances. Biologically active and valuable chemical substances can be obtained both, as independent end products of mycelium cultivation, as well as by-products, for example, of the industrial production of food or stern biomass. Our studies were devoted to the search of some proteolytic enzymes produced by higher basidiomycetes during submerge cultivation, namely milk-clotting, fibrinolytic and thrombolytic enzymes. With the production of cheeses the key feature for the successful decision of technological process is the selection of the milk-clotting enzyme. The rennet (rennin, chymosin), produced in the abonasum (division of stomach) of young ruminant animals, was used by millennia in the cheese making for milk coagulation. The replacement of the expensive rennet by microbial proteases of specific action is economically advantageous, promising and is always urgent Requirements for the substitutes of the rennet are strict and specific—their enzymatic properties must maximally approach those of accepted as the standard natural rennin, i.e. together with the high milk-clotting activity they must possess the insignificant general proteolytic activity, which leads to the unspecific proteolysis of the proteins of casein. Milk-clotting enzymes were purified and characterized from the native liquids of several mushrooms. Lyophilized active fractions possess the high levels of milk-clotting activity. Enzymes have molecular weight of 37–41 kDa, temperature optimum 34–37 ◦ C, the optimum of pH 6.4–6.5. The use of this enzyme preparations as the milk-clotting agent led to the formation of dense milk clusters without the aftertaste of bitterness. It was very interesting to found, that the same fractions of native liquid which was actively clotting milk, possess significant fibrinolytic activity. In vivo experiments on Wistar male rats also demonstrates the ability of the purified preparations injected intravenously, efficiently to solve the thrombus in venues and arteries of experimental animals.
Reference
doi:10.1016/j.jbiotec.2008.07.1884
Saraswat, V., Bisaria, V.S., 1997. Biosynthesis of xylanolytic and xylan debranching enzymes in Melanocarpus albomyces IIS 68. J. Ferment. Bioeng. 83, 352–357.
V1-P-002
doi:10.1016/j.jbiotec.2008.07.1883
Exopolysaccharide production in batch and semi-continuous fermentation of Cordyceps sinensis
Ranjita Biswas ∗ , Vikram Sahai, Saroj Mishra, Virendra S. Bisaria Department of Biochemical Engineering & Biotechnology, Indian Institute of Technology Delhi, New Delhi, India
Yuan-Shuai Liu ∗ , Po-Hong Leung, Jian-Yong Wu Department of Applied Biology & Chemical Technology, the Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong E-mail address: [email protected] (Y.-S. Liu). Cordyceps sinensis (Berk.) Sacc., known as DongChongXiaCao in Chinese, is a precious medicinal fungus. Polysaccharides (PS) represent a major class of the bioactive compounds of Cordyceps and