Insight into the protein thermostability based on comparison of catalytic pocket of bacterial chitinases

Publish Year: 1397
نوع سند: مقاله کنفرانسی
زبان: English
View: 351

نسخه کامل این Paper ارائه نشده است و در دسترس نمی باشد

  • Certificate
  • من نویسنده این مقاله هستم

استخراج به نرم افزارهای پژوهشی:

لینک ثابت به این Paper:

شناسه ملی سند علمی:

IBIS08_051

تاریخ نمایه سازی: 9 مرداد 1398

Abstract:

Chitin is the second most abundant biopolymer on the earth after cellulose .Chitinases are glycosyl hydrolases that catalyze the conversion of chitin biopolymer to low molecular weight chitooligomers which have wide variety of biotechnological and industrial applications [1-2]. In present study we compare some important physiochemical properties of catalytic domain and active site pocket of psychrophilic, mesophilic and thermophilic chitinases. The catalytic domains were retrieved from Interpro database. The 3-D models of various types of chitinases were predicted using Modeller 9 & 15 software [3]. Then, the quality of the models were evaluated with PROCHECK and PROSA II servers. The active pocketes predicted using CastP and Ftsite servers. The physiochemical properties of mesophilic and thermophilic chitinases were compared. Our result showed cysteine and aspartic acid are two important residues that affect the thermal resistance of enzymes.

Keywords:

Chitinase , homology modeling and Active Pocket

Authors

وجیهه اسکندری

دانشگاه زنجان