ArticleBiotechnology for biofuels2021
Improvements of the productivity and saccharification efficiency of the cellulolytic β-glucosidase D2-BGL in Pichia pastoris via directed evolution.
Article in Biotechnology for biofuels, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 34 citations in OpenAlex.
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- Installing xylose assimilation and cellodextrin phosphorolysis pathways in obese Yarrowia lipolytica facilitates cost-effective lipid production from lignocellulosic hydrolysates.Biotechnology for biofuels and bioproducts · 2023Article
- Engineering the Metabolic Landscape of Microorganisms for Lignocellulosic Conversion.Microorganisms · 2023Review
- Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review.Molecules (Basel, Switzerland) · 2023Review
- Latent generative landscapes as maps of functional diversity in protein sequence space.Nature communications · 2023Article
- Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023Review
- Mutation Hotspot for Changing the Substrate Specificity of β-International journal of molecular sciences · 2022Article
- Characterization of a GH5 endoxylanase from Penicillium funiculosum and its synergism with GH16 endo-1,3(4)-glucanase in saccharification of sugarcane bagasse.Scientific reports · 2022Article
- Engineering a carbohydrate-binding module to increase the expression level of glucoamylase in Pichia pastoris.Microbial cell factories · 2022Article
- Fungal cellulases: protein engineering and post-translational modifications.Applied microbiology and biotechnology · 2022Review
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3 authors at 2 institutions in 1 country.
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Abstract
backgroundβ-Glucosidases are essential for cellulose hydrolysis by catalyzing the final cellulolytic degradation of cello-oligomers and cellobiose to glucose. D2-BGL is a fungal glycoside hydrolase family 3 (GH3) β-glucosidase isolated from Chaetomella raphigera with high substrate affinity, and is an efficient β-glucosidase supplement to Trichoderma reesei cellulase mixtures for the saccharification of lignocellulosic biomass.
resultsWe have carried out error-prone PCR to further increase catalytic efficiency of wild-type (WT) D2-BGL. Three mutants, each with substitution of two amino acids on D2-BGL, exhibited increased activity in a preliminary mutant screening in Saccharomyces cerevisiae. Effects of single amino acid replacements on catalysis efficiency and enzyme production have been investigated by subsequent expression in Pichia pastoris. Substitution F256M resulted in enhancing the tolerance to substrate inhibition and specific activity, and substitution D224G resulted in increasing the production of recombinant enzyme. The best D2-BGL mutant generated, Mut M, was constructed by combining beneficial mutations D224G, F256M and Y260D. Expression of Mut M in Pichia pastoris resulted in 2.7-fold higher production of recombinant protein, higher V
conclusionsD2-BGL mutant Mut M was generated successfully by following directed evolution approach. Mut M carries three mutations that are not reported in other directed evolution studies of GH3 β-glucosidases, and this mutant exhibited greater tolerance to substrate inhibition and higher V
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