24 research outputs found
Production of a bacterial cellulose/poly(3-hydroxybutyrate) blend activated with clove essential oil for food packaging
Optimization of a novel coconut milk supplemented dahi - a fermented milk product of Indian subcontinent
Molecular characterization of an exopolysaccharide from a probiotic Lactobacillus plantarum MTCC 9510 and its efficacy to improve the texture of starchy food
Effect of carbon and nitrogen sources on simultaneous production of α-amylase and green food packaging polymer by Bacillus sp. CFR 67
An overview of fungal biopolymers: bioemulsifiers and biosurfactants compounds production
Utilization of palm oil mill effluent for polyhydroxyalkanoate production and nutrient removal using statistical design
Hypocholesterolemic Effect of Potential Probiotic Lactobacillus fermentum Strains Isolated from Traditional Fermented Foods in Wistar Rats
Statistical optimization of process parameters for exopolysaccharide production by Aureobasidium pullulans using sweet potato based medium
Synergistic effect of mutagenesis and truncation to improve a polyesterase from Clostridium botulinum for polyester hydrolysis
Abstract The activity of the esterase (Cbotu_EstA) from Clostridium botulinum on the polyester poly(ethylene terephthalate) (PET) was improved by concomitant engineering of two different domains. On the one hand, the zinc-binding domain present in Cbotu_EstA was subjected to site-directed mutagenesis. On the other hand, a specific domain consisting of 71 amino acids at the N-terminus of the enzyme was deleted. Interestingly, a combination of substitution of residues present in the zinc-binding domain (e.g. S199A) synergistically increased the activity of the enzyme on PET seven fold when combined to the truncation of 71 amino acids at the N-terminus of the enzyme only. Overall, when compared to the native enzyme, the combination of truncation and substitutions in the zinc-binding domain lead to a 50-fold activity improvement. Moreover, analysis of the kinetic parameters of the Cbotu_EstA variants indicated a clear shift of activity from water soluble (i.e. para-nitrophenyl butyrate) to insoluble polymeric substrates. These results evidently show that the interaction with non-natural polymeric substrates provides targets for enzyme engineering