portant Discovery: Bifunctional Enzyme Unveils Dual-Substrate Recognition and Catalytic Mechanisms

The innovative team of food enzyme engineering from the Institute of Agro-Products Processing, Chinese Academy of Agricultural Sciences, has recently published an impactful research paper "Structural Insights into the Dual-Substrate Recognition and Catalytic Mechanisms of a Bifunctional Acetyl Ester-Xyloside Hydrolase from Caldicellulosiruptor lactoaceticus" in ACS Catalysis, a catalysis field journal under the American Chemical Society. The study identified a bifunctional hydrolase, CLH10, that can efficiently hydrolyze both the β-1,4-xylosidic bond of the main chain and the acetyl ester bond of the side chains of xylooligosaccharides. More importantly, the study elucidated the molecular mechanisms underlying the dual-substrate recognition and catalytic functionalities of CLH10, which are accomplished within a single protein structural domain.

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