A mutant strain T199 producing about 8 times as much β-glucanase as its parent strain trichoderma kningii T3 was obtained by treatment with ultraviolet light and N-methyl-N-nitro-N-nitrosoguanidine.Fermentation was...A mutant strain T199 producing about 8 times as much β-glucanase as its parent strain trichoderma kningii T3 was obtained by treatment with ultraviolet light and N-methyl-N-nitro-N-nitrosoguanidine.Fermentation was conducted in 250mL flask,each containing 30mL of medium consisted of 5% corn cob powder,3% wheat bran and 1.4% nitrogen source No.10 ((NH 4) 2SO 4 10%,Peptone 20%,Yeast extract 15%).The optima culture conditions were as below:initial pH5.0,30℃,shaking speed 280r/min,and cultivation time 5d.Enzyme activity toward CMC-Na,lichenin,laminarin and barley β-glucan at pH 5.0 and 60℃ for 10min were 300,1100,12 and 1600 IU/mL,respectively.The optima pH and temperature for enzyme action toward barley β-glucan were pH 5.0 and 70℃,respectively.The enzyme was stable under below 50℃ and at pH 4.5～6.5.展开更多
Objective To prepare an active anti-tumor component,compound K(C-K),from saponins in leaves of Panax notoginseng(SLPN) using immobilized β-glucanase.Methods Two entrapments,alginate gel-1(Alg 1) and alginate gel-2(Al...Objective To prepare an active anti-tumor component,compound K(C-K),from saponins in leaves of Panax notoginseng(SLPN) using immobilized β-glucanase.Methods Two entrapments,alginate gel-1(Alg 1) and alginate gel-2(Alg 2),were evaluated for their ability to immobilize β-glucanase.The amount and purity of C-K obtained from the transformation process were analyzed by HPLC,and the immobilizing parameters were optimized.Results β-Glucanase can be immobilized and reused with either of the entrapment.However,using Alg 1 resulted in higher enzyme activity than Alg 2.The optimal concentration of the immobilized enzyme was 10%;The optimal crosslinking time was 4–6 h;and the optimal concentration of the crosslinking agent was 6%– 7%.Conclusion Immobilized β-glucanase shows sustained enzyme activity,good ethanol tolerance,and was reusable for the preparation of C-K from SLPN.展开更多
文摘A mutant strain T199 producing about 8 times as much β-glucanase as its parent strain trichoderma kningii T3 was obtained by treatment with ultraviolet light and N-methyl-N-nitro-N-nitrosoguanidine.Fermentation was conducted in 250mL flask,each containing 30mL of medium consisted of 5% corn cob powder,3% wheat bran and 1.4% nitrogen source No.10 ((NH 4) 2SO 4 10%,Peptone 20%,Yeast extract 15%).The optima culture conditions were as below:initial pH5.0,30℃,shaking speed 280r/min,and cultivation time 5d.Enzyme activity toward CMC-Na,lichenin,laminarin and barley β-glucan at pH 5.0 and 60℃ for 10min were 300,1100,12 and 1600 IU/mL,respectively.The optima pH and temperature for enzyme action toward barley β-glucan were pH 5.0 and 70℃,respectively.The enzyme was stable under below 50℃ and at pH 4.5～6.5.
基金ZHAO Yu-qing was supportive with a Liaoning Modernization TCM grant (LN403004),China
文摘Objective To prepare an active anti-tumor component,compound K(C-K),from saponins in leaves of Panax notoginseng(SLPN) using immobilized β-glucanase.Methods Two entrapments,alginate gel-1(Alg 1) and alginate gel-2(Alg 2),were evaluated for their ability to immobilize β-glucanase.The amount and purity of C-K obtained from the transformation process were analyzed by HPLC,and the immobilizing parameters were optimized.Results β-Glucanase can be immobilized and reused with either of the entrapment.However,using Alg 1 resulted in higher enzyme activity than Alg 2.The optimal concentration of the immobilized enzyme was 10%;The optimal crosslinking time was 4–6 h;and the optimal concentration of the crosslinking agent was 6%– 7%.Conclusion Immobilized β-glucanase shows sustained enzyme activity,good ethanol tolerance,and was reusable for the preparation of C-K from SLPN.
