AI Article Synopsis
- * The process of elongation and branching in β-1,3-glucans involves specific enzymes called β-1,3-glucantransferases from GH72 or GH17 families, which modify the glucan chains by breaking and reattaching segments.
- * This review highlights the structural details and functions of these enzymes, aiming to improve understanding of β-1,3-glucan biosynthesis and inform strategies for producing more effective branched or elongated glucans.
Article Abstract
β-1,3-Glucans form the major carbohydrate component of fungal cell walls, playing a vital role in cell viability, stress response, virulence, and even healthy functions such as immuno-enhancement. The elongation and branching of β-1,3-glucans is a mystery. More evidence proved the β-1, 3-glucantransferases belonging to GH72 or GH17 family to branch and remodel the synthesized linear β-1, 3-glucan chain by cleaving its internal β-1, 3-linkage and transfer the cleaved fragment to the nonreducing end of another β-1, 3-glucan acceptor. The present review summarized the comprehensive advances of β-1, 3-glucantransferases including their structures such as catalytic and non-catalytic protein domains, catalytic mechanisms and roles in cell wall formation, cell separation and cell viability to provide the references for understanding and guiding the biosynthesis and production regulation of functional β-1, 3-glucans with high-branched or elongated structures.
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| http://dx.doi.org/10.1016/j.ijbiomac.2024.138651 | DOI Listing |
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