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Marquez-Rios, Enrique,Cota-Arriola, Octavio,Villalba-Villalba, Ana Gloria,Ezquerra-Brauer, Josafat Marina,Ocano-Higuera, Victor Manuel,Lopez-Corona, Betzabe Ebenhezer,Torres-Arreola, Wilfrido 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.4
Chymotrypsin was purified from jumbo squid hepatopancreas (HP) with 2.4-fold and yield 1.9%, and characterized with a molecular weight of 31 kDa, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Chymotrypsin effect over collagen extracted from the mantle, fins and arms of the jumbo squid was evaluated. The enzyme exhibited the maximum activity at pH 7 and $65^{\circ}C$ using Suc-Ala-Ala-Pro-Phe-p-nitroanilide (SAAPNA) as a substrate and it was identified using the specific inhibitors N-tosyl-L-phenylalaninechloromethyl ketone (TPCK) and phenyl methyl sulfonyl fluoride (PMSF), showing residual activities of 6% and 0%, respectively. Furthermore, high activity was observed in the pH range of 4.0 to 8.0. Purified enzyme showed a moderate in vitro activity using muscle collagen as a substrate. Although further research is needed, the results suggest that the enzyme has a potential application where acidic or slightly alkaline conditions are needed.
Enrique Marquez-Rios,Octavio Cota-Arriola,Ana Gloria Villalba-Villalba,Josafat Marina Ezquerra-Brauer,Victor Manuel Ocaño-Higuera,Betzabe Ebenhezer Lopez-Corona,Wilfrido Torres-Arreola 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.4
Chymotrypsin was purified from jumbo squid hepatopancreas (HP) with 2.4-fold and yield1.9%, and characterized with a molecular weight of 31 kDa, as estimated by sodium dodecyl sulfatepolyacrylamidegel electrophoresis (SDS-PAGE). Chymotrypsin effect over collagen extracted from themantle, fins and arms of the jumbo squid was evaluated. The enzyme exhibited the maximum activityat pH 7 and 65oC using Suc-Ala-Ala-Pro-Phe-p-nitroanilide (SAAPNA) as a substrate and it was identifiedusing the specific inhibitors N-tosyl-L-phenylalaninechloromethyl ketone (TPCK) and phenyl methylsulfonyl fluoride (PMSF), showing residual activities of 6% and 0%, respectively. Furthermore, highactivity was observed in the pH range of 4.0 to 8.0. Purified enzyme showed a moderate in vitro activityusing muscle collagen as a substrate. Although further research is needed, the results suggest that theenzyme has a potential application where acidic or slightly alkaline conditions are needed.