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- W3039233677 abstract "Abstract Dissociation of non-productively 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 non-productive enzyme binding is not well understood. Here, we examine the subtle interplay of CBM binding and cellulose hydrolysis activity for three model Type-A CBMs (families 1, 3a, and 64) tethered to a 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 (QCM-D) 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 non-productive enzyme binding and develop improved cellulolytic enzymes for industrial applications." @default.
- W3039233677 created "2020-07-10" @default.
- W3039233677 creator A5008781513 @default.
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- W3039233677 creator A5031253432 @default.
- W3039233677 date "2020-07-03" @default.
- W3039233677 modified "2023-10-18" @default.
- W3039233677 title "Reduced Type-A Carbohydrate-Binding Module Interactions to Cellulose Leads to Improved Endocellulase Activity" @default.
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- W3039233677 doi "https://doi.org/10.1101/2020.07.02.183293" @default.
- W3039233677 hasPublicationYear "2020" @default.
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