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PreprintCited by 55Enzyme Production and CharacterizationEnzyme Catalysis and ImmobilizationBiofuel production and bioconversion

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Recent Advances in β-glucosidase Engineering: A Brief Review

Open access
Zhao, Xihua, Huang, Yunhong, Ouyang, Bei, Wang, Guoping, Zhang, Nian, Zuo, Jiali·2023·Molecules
DOI 10.20944/preprints202306.0235.v1PMC PMC10343665

Preprint — published as 10.3390/molecules28134990 · Paper page

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Abstract

β-glucosidases (BGLs) play a crucial role in the degradation of lignocellulosic biomass as well as in industrial applications such as pharmaceuticals, foods, and flavors. However, the application of BGLs has been largely hindered by issues such as low enzyme activity, product inhibition, low stability, etc. Many approaches have been developed to engineer BGLs to improve these enzymatic characteristics to facilitate industrial production. In this article, we review the recent advances in BGL engineering in the field, including the efforts from our laboratory. We summarize and discuss the BGL engineering studies according to the targeted functions as well as the specific strategies used for BGL engineering.

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Crossref · 10.20944/preprints202306.0235.v1

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Figures

Figure 1 The three-dimensional structure of BGL. (A) Structure of PcBGL1A (PDB ID: 2e3z) from the GH1 Phanerodontia chrysosporium with α-helices, β-sheets, and loops shown in red, yellow, and green, respectively. (B) Structure model of 16BGL from the GH3 Penicillium oxalicum with α-helices, β-sheets, and loops shown in red, yellow, and green, respectively. The FnIII domain of unknown function is shown in blue.
Figure 1 The three-dimensional structure of BGL. (A) Structure of PcBGL1A (PDB ID: 2e3z) from the GH1 Phanerodontia chrysosporium with α-helices, β-sheets, and loops shown in red, yellow, and green, respectively. (B) Structure model of 16BGL from the GH3 Penicillium oxalicum with α-helices, β-sheets, and loops shown in red, yellow, and green, respectively. The FnIII domain of unknown function is shown in blue.CC BY · PubMed Central
Figure 2 Reaction mechanism of BGL. (A) The “inversion” mechanism. (B) The “retention” mechanism. Both the leaving group (R) and the acceptor (A) are different glycosyl molecules.
Figure 2 Reaction mechanism of BGL. (A) The “inversion” mechanism. (B) The “retention” mechanism. Both the leaving group (R) and the acceptor (A) are different glycosyl molecules.CC BY · PubMed Central
Figure 3 Directed evolution, computer-aided rational design and semi-rational design strategies for enzyme engineering.
Figure 3 Directed evolution, computer-aided rational design and semi-rational design strategies for enzyme engineering.CC BY · PubMed Central

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Metadata

Authors
Zhao, X., Huang, Y., Ouyang, B., Wang, G., Zhang, N., & Zuo, J.
Affiliations
Jiangxi Normal University (CN)
Corresponding author
  • Zhao, Xihua
  • Huang, Yunhong
ORCID
Venue
Molecules
Publisher
MDPI AG
Published
2023-06-05
Volume
28
Issue
13
Pages
4990-4990
ISSN
1420-3049 (ISSN-L)
DOI
10.20944/preprints202306.0235.v1
PMC
PMC10343665
OpenAlex
W4382060579
Cited by
55
References
1
Citations by year
2026: 18 · 2025: 18 · 2024: 17 · 2023: 2
FWCI
1.64
Type
journal article
Language
en
Open access
Licence
Locations
  • Molecules (publishedVersion, cc-by)
  • Preprints.org (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • University of Michigan
  • National Natural Science Foundation of China (22068014, 21666010)
  • Jiangxi Normal University
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Physical Sciences › Engineering › Biomedical Engineering › Biofuel production and bioconversion
Keywords
β-glucosidase, enzyme engineering, lignocellulose degradation, enzyme stability, product inhibition, enzyme activity enhancement, industrial enzymes, sequence engineering, structural engineering
MeSH terms
beta-Glucosidase

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