ArticleApplied microbiology and biotechnology2020
Enhancing cellulosic ethanol production through coevolution of multiple enzymatic characteristics of β-glucosidase from Penicillium oxalicum 16.
Article in Applied microbiology and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 20 citations in OpenAlex.
- Structure-coevolution dual-guided engineering of C-glycosyltransferase enables high-level biosynthesis of vitexin inSynthetic and systems biotechnology · 2026Article
- Optimizing Bioaugmentation for Pharmaceutical Stabilization of Sewage Sludge: A Study on Short-Term Composting Under Real Conditions.Journal of fungi (Basel, Switzerland) · 2025Article
- A thermostable and inhibitor resistant β-glucosidase from Rasamsonia emersonii for efficient hydrolysis of lignocellulosics biomass.Bioprocess and biosystems engineering · 2024Article
- Characterization of a novel cold-adapted GH1 β-glucosidase fromCurrent research in food science · 2024Article
- Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review.Molecules (Basel, Switzerland) · 2023Review
- Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A fromBiomolecules · 2021Article
- Comparative Secretomics Analysis Reveals the Major Components ofMicroorganisms · 2021Article
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5 authors at 1 institution in 1 country.
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Abstract
In previous studies, we isolated a novel β-glucosidase from Penicillium oxalicum 16 (16BGL), which is useful for producing cellulosic ethanol. However, 16BGL has a relatively low enzyme activity and product tolerance; besides, a huge gap exists between the optimum temperature of 16BGL (70 °C) and the fermentation temperature for producing cellulosic ethanol (40 °C). Here, we present a directed evolution-based study, which combines one-round error-prone PCR with three rounds of high-throughput screening, for coevolving multiple enzymatic characteristics of 16BGL. We identified an improved variant Y-1-B1 with a triple mutant (G414S/D421V/T441S). Y-1-B1 had an optimum temperature of 50 °C, much closer to the fermentation temperature. The catalytic efficiency of Y-1-B1 for hydrolyzing pNPG was 1355 mM
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