2024
DOI: 10.1016/j.enzmictec.2023.110363
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Exploring the diversity of β-glucosidase: Classification, catalytic mechanism, molecular characteristics, kinetic models, and applications

Mehmet Emre Erkanli,
Khalid El-Halabi,
Jin Ryoun Kim
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Cited by 12 publications
(6 citation statements)
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“…The impacts of the Q214S/A264S/F344I mutations on the contact probabilities with other active site residues differed depending on the protein chains though no general chain‐dependent trend was found. An enzyme with broad substrate specificity, such as GH1 glycoside hydrolases including PfBGL (Chen et al, 2022; Erkanli et al, 2024), was proposed to exhibit high native state flexibility around the active site, which is related to the distribution of conformational substates (St‐Jacques et al, 2023; Wintrode & Arnold, 2000). Hence, the Q214S/A264S/F344I mutations may readily reshape the dynamic conformational landscape around the active site, by enriching catalytically productive substates and depopulating nonproductive substates upon substrate binding, leading to the increased β‐glucosidase activity (Bian et al, 2016; Kaczmarski et al, 2020; St‐Jacques et al, 2023).…”
Section: Discussionmentioning
confidence: 99%
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“…The impacts of the Q214S/A264S/F344I mutations on the contact probabilities with other active site residues differed depending on the protein chains though no general chain‐dependent trend was found. An enzyme with broad substrate specificity, such as GH1 glycoside hydrolases including PfBGL (Chen et al, 2022; Erkanli et al, 2024), was proposed to exhibit high native state flexibility around the active site, which is related to the distribution of conformational substates (St‐Jacques et al, 2023; Wintrode & Arnold, 2000). Hence, the Q214S/A264S/F344I mutations may readily reshape the dynamic conformational landscape around the active site, by enriching catalytically productive substates and depopulating nonproductive substates upon substrate binding, leading to the increased β‐glucosidase activity (Bian et al, 2016; Kaczmarski et al, 2020; St‐Jacques et al, 2023).…”
Section: Discussionmentioning
confidence: 99%
“…The conversion of the pretreated cellulose into small oligo-saccharides and, eventually, into glucoses, requires the complementary and synergetic actions of the three enzymes that make up cellulase: exoglucanase, endoglucanase, and β-glucosidase (Banerjee et al, 2010). Accordingly, commercial cellulases (e.g., Cellic ® Ctec3 from Novozymes) are produced and provided in a hydrolytic cocktail containing the three enzymes (Erkanli et al, 2024). In the enzyme mixtures, endoglucanase randomly cleaves the long polymeric cellulose chains, creating shorter oligomeric chains for subsequent degradations.…”
Section: Introductionmentioning
confidence: 99%
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“…Cellobiose and xylan also inhibit cellobiohydrolases and cellulases, respectively. Notably, studies have found that, under certain conditions, xylose at low concentrations can stimulate β-glucosidases with doubled hydrolytic activity, while the binding of cellobiose to the active site of the enzyme may be interfered by high xylose concentrations [171]. This phenomenon implies the need for precise control over the effects of different components on enzyme activity for saccharification condition optimization and efficiency improvement.…”
Section: Saccharification Processmentioning
confidence: 99%