I recently read an online article on the publication of a research paper titled "Structural Insights into the Dual-Substrate Recognition and Catalytic Mechanisms of a Bifunctional Acetyl Ester-Xyloside Hydrolase from Caldicellulosiruptor lactoaceticus" by the food enzyme engineering innovation team at the Agricultural Product Processing Institute of the Chinese Academy of Agricultural Sciences. The research paper was published in the catalysis fields journal "ACS Catalysis" under the American Chemical Society. The paper revealed a new type of bifunctional hydrolytic enzyme called CLH10, which can simultaneously hydrolyze both the main chain (β-1,4-xyloside bond) and side chain (acetyl ester bond) of xylan. It also exposed how the enzyme uses a single sequence domain to recognize two different substrates and catalyze two different reaction types by revealing the molecular mechanism. The research paper itself was very informative and insightful, and I feel that it will truly help advance the field and our understanding of bifunctional hydrolytic enzymes.After stumbling upon an article online, I came across a topic that sparked my interest - "Green Manufacturing". It is an essential and necessary path to achieving sustainable development and it's also a significant requirement for our country's major strategic needs. In the agricultural industry, the processing of various materials such as xylan is still a huge challenge as it results in structurally complex byproducts that are difficult to be effectively utilized. Xylan is an essential biomass resource, and its hierarchical utilization is a practical way to achieve high-value utilization in agricultural product processing. However, due to the network structure formed by the main chain and side chain of xylan, complex multi-enzyme cooperative catalysis is required to achieve efficient degradation and utilization. That's where CLH10 comes in, with its ability to simultaneously hydrolyze the main chain and acetyl ester side chain of xylan, it has the potential for high-efficient enzymatic degradation of xylan with many applications. Through crystal structure analysis, bioinformatics analysis, and enzyme kinetics research, we have discovered that CLH10 contains discrete staggered esterase and glycoside conservative sequence fragments in its primary sequence structure. Its unique structure is what allows it to have the potential to be both a highly efficient and multi-use enzyme for the degradation of xylan.As a reader, I find it fascinating to learn about a new study regarding a novel hydrolytic enzyme with dual functionality. The research has provided a detailed understanding of how the enzyme, CLH10, has acquired the extraordinary ability to recognize and catalyze two independent substrates, acetyl ester, and xyloglucan, through sequence folding. The dual functionality of CLH10 is significant as it displays catalytic independence. The structural and evolutionary behavior analysis has shown that CLH10 has obtained the capacity to identify and catalyze xyloglucan in its Loop region while preserving its esterase protective catalysis function. This scientific research has provided a new perspective on how to design and evolve enzymes with multiple catalytic functions.

It’s worth mentioning that this study has received support from various sources, including the Chinese Academy of Agricultural Sciences Technology Innovation Project, the National Key Research and Development Program of China (2017YFD0400204), the National Natural Science Foundation of China (31801475, 31700701), and China Postdoctoral Science Foundation (2018M630230). The corresponding authors of this study are research fellows Fengjiao Xin and Fengzhong Wang, and the co-first authors are postdoctoral fellow Hao Cao and assistant research fellow Lichao Sun.I came across an interesting link that I wanted to share with others. This link provides access to the original article "A novel bifunctional xyloglucan-specific acetyl esterase from Penicillium chrysogenum P33 with activity on branched and Linear Acetyl Xyloglucan Oligosaccharides." The article is published on the website https://ifst.caas.cn//pubs.acs.org/doi/10.1021/acscatal.8b03383 and it is an insightful read that sheds light on a new dual-functional enzyme, CLH10. This enzyme combines the capability to detect and degrade xyloglucan and acetyl ester, which provides an opportunity to discover more about its dual catalysis mechanism. This article is a valuable resource and provides a new perspective on designing and evolving enzymes with multiple catalytic functions.