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Catalytic efficiency of chitinase-D on insoluble chitinous substrates was improved by fusing auxiliary domains.

التفاصيل البيبلوغرافية
العنوان: Catalytic efficiency of chitinase-D on insoluble chitinous substrates was improved by fusing auxiliary domains.
المؤلفون: Jogi Madhuprakash, Nour Eddine El Gueddari, Bruno M Moerschbacher, Appa Rao Podile
المصدر: PLoS ONE, Vol 10, Iss 1, p e0116823 (2015)
بيانات النشر: Public Library of Science (PLoS), 2015.
سنة النشر: 2015
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: Chitin is an abundant renewable polysaccharide, next only to cellulose. Chitinases are important for effective utilization of this biopolymer. Chitinase D from Serratia proteamaculans (SpChiD) is a single domain chitinase with both hydrolytic and transglycosylation (TG) activities. SpChiD had less of hydrolytic activity on insoluble polymeric chitin substrates due to the absence of auxiliary binding domains. We improved catalytic efficiency of SpChiD in degradation of insoluble chitin substrates by fusing with auxiliary domains like polycystic kidney disease (PKD) domain and chitin binding protein 21 (CBP21). Of the six different SpChiD fusion chimeras, two C-terminal fusions viz. ChiD+PKD and ChiD+CBP resulted in improved hydrolytic activity on α- and β-chitin, respectively. Time-course degradation of colloidal chitin also confirmed that these two C-terminal SpChiD fusion chimeras were more active than other chimeras. More TG products were produced for a longer duration by the fusion chimeras ChiD+PKD and PKD+ChiD+CBP.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: http://europepmc.org/articles/PMC4304778?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0116823
URL الوصول: https://doaj.org/article/d160f12a3e584e6db3cb4389aeffd4c5
رقم الأكسشن: edsdoj.160f12a3e584e6db3cb4389aeffd4c5
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0116823