AI Article Synopsis
- The study compares the enzymatic activity of a specific β-1,4-D-endoglucanase (MeCel45A) from blue mussels with other enzymes in the glycoside hydrolase family 45, focusing on their efficiency in hydrolyzing barley beta-glucan, konjac glucomannan, and carboxymethyl cellulose.
- The crystal structure of MeCel45A is documented, revealing its unique features and performance, especially in colder temperatures where it retains high activity levels.
- While all enzymes exhibit inverting glycoside hydrolase activity, MeCel45A and the C subfamily enzymes show mannanase activity, while subfamily A yielded glucose, showcasing distinct functionalities among these
Article Abstract
The enzymatic hydrolysis of barley beta-glucan, konjac glucomannan and carboxymethyl cellulose by a β-1,4-D-endoglucanase MeCel45A from blue mussel, Mytilus edulis, which belongs to subfamily B of glycoside hydrolase family 45 (GH45), was compared with GH45 members of subfamilies A (Humicola insolens HiCel45A), B (Trichoderma reesei TrCel45A) and C (Phanerochaete chrysosporium PcCel45A). Furthermore, the crystal structure of MeCel45A is reported. Initial rates and hydrolysis yields were determined by reducing sugar assays and product formation was characterized using NMR spectroscopy. The subfamily B and C enzymes exhibited mannanase activity, whereas the subfamily A member was uniquely able to produce monomeric glucose. All enzymes were confirmed to be inverting glycoside hydrolases. MeCel45A appears to be cold adapted by evolution, as it maintained 70% activity on cellohexaose at 4 °C relative to 30 °C, compared to 35% for TrCel45A. Both enzymes produced cellobiose and cellotetraose from cellohexaose, but TrCel45A additionally produced cellotriose.
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| http://dx.doi.org/10.1016/j.carbpol.2021.118771 | DOI Listing |
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