甲壳素
哈维氏弧菌
几丁质酶
化学
吸附
基质(水族馆)
降级(电信)
壳聚糖
酶
微生物学
弧菌
生物化学
核化学
细菌
有机化学
生物
生态学
电信
遗传学
计算机科学
作者
Qiao Zhang,Xueying Zhang,Yuanchang He,Yongcheng Li
标识
DOI:10.1016/j.carbpol.2023.120640
摘要
In this study, two chitinases (VhChit2 and VhChit6) from Vibrio harveyi possessed specific activity of 36.5 and 20.8 U/mg, respectively. Structure analysis indicates that their amino acid composition of active sites is similar, but the substrate binding cleft of VhChit2 is deeper than that of VhChit6. They were shown to have a synergistic effect on chitin degradation, and the optimized degree of synergy and the degradation ratio of chitin reached 1.75 and 23.6 %, respectively. The saturated adsorption capacity of VhChit2 and VhChit6 adsorbed in 1 g of chitin was 48.5 and 33.4 mg. It was found that VhChit2 and VhChit6 had different adsorption sites on chitin, making more enzymes absorbed by chitin. Furthermore, the combined use of VhChit2 and VhChit6 increased their binding force of chitinases with the substrate. The synergistic action of VhChit2 and VhChit6 may be attributed to their different adsorption sites on chitin and the increased binding force with chitin.
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