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Reduced type-A carbohydrate-binding module interactions to cellulose I leads to improved endocellulase activity.

التفاصيل البيبلوغرافية
العنوان: Reduced type-A carbohydrate-binding module interactions to cellulose I leads to improved endocellulase activity.
المؤلفون: Nemmaru B, Ramirez N; Department of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA., Farino CJ; Department of Biomedical Engineering, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA., Yarbrough JM; Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA., Kravchenko N; Department of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA., Chundawat SPS; Department of Chemical and Biochemical Engineering, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA.
المصدر: Biotechnology and bioengineering [Biotechnol Bioeng] 2021 Mar; Vol. 118 (3), pp. 1141-1151. Date of Electronic Publication: 2020 Dec 16.
نوع المنشور: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Wiley Country of Publication: United States NLM ID: 7502021 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-0290 (Electronic) Linking ISSN: 00063592 NLM ISO Abbreviation: Biotechnol Bioeng Subsets: MEDLINE
أسماء مطبوعة: Publication: <2005->: Hoboken, NJ : Wiley
Original Publication: New York, Wiley.
مواضيع طبية MeSH: Cellulases/*chemistry , Cellulose/*chemistry, Hydrolysis ; Protein Binding
مستخلص: Dissociation of nonproductively bound cellulolytic enzymes from cellulose is hypothesized to be a key rate-limiting factor impeding cost-effective biomass conversion to fermentable sugars. However, the role of carbohydrate-binding modules (CBMs) in enabling nonproductive enzyme binding is not well understood. Here, we examine the subtle interplay of CBM binding and cellulose hydrolysis activity for three models type-A CBMs (Families 1, 3a, and 64) tethered to multifunctional endoglucanase (CelE) on two distinct cellulose allomorphs (i.e., cellulose I and III). We generated a small library of mutant CBMs with varying cellulose affinity, as determined by equilibrium binding assays, followed by monitoring cellulose hydrolysis activity of CelE-CBM fusion constructs. Finally, kinetic binding assays using quartz crystal microbalance with dissipation were employed to measure CBM adsorption and desorption rate constants k on and k off , respectively, towards nanocrystalline cellulose derived from both allomorphs. Overall, our results indicate that reduced CBM equilibrium binding affinity towards cellulose I alone, resulting from increased desorption rates ( k off ) and reduced effective adsorption rates ( nk on ), is correlated to overall improved endocellulase activity. Future studies could employ similar approaches to unravel the role of CBMs in nonproductive enzyme binding and develop improved cellulolytic enzymes for industrial applications.
(© 2020 Wiley Periodicals LLC.)
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فهرسة مساهمة: Keywords: carbohydrate-binding module; cellulose III; endocellulases; nonproductive binding; protein adsorption; quartz crystal microbalance with dissipation
المشرفين على المادة: 9004-34-6 (Cellulose)
EC 3.2.1.- (Cellulases)
تواريخ الأحداث: Date Created: 20201127 Date Completed: 20220117 Latest Revision: 20220117
رمز التحديث: 20221213
DOI: 10.1002/bit.27637
PMID: 33245142
قاعدة البيانات: MEDLINE
الوصف
تدمد:1097-0290
DOI:10.1002/bit.27637