裂解性多糖单加氧酶驱动不同结构甲壳素降解的研究  

Researches on the Biotransformation of Chitin with Different Structures Catalyzed by Lytic Polysaccharide Monooxygenase

作　　者：毛相朝[1,2,3,4] 赵红军 苏海鹏 吕晓晓 孙建安 Mao Xiangzhao;Zhao Hongjun;Su Haipeng;Lv Xiaoxiao;Sun Jian’an(State Key Laboratory of Marine Food Processing and Safety Control,College of Food Science and Engineering,Ocean University of China,Qingdao 266404,China;Laboratory for Marine Drugs and Bioproducts,Qingdao Marine Science and Technology Center,Qingdao 266237,China;Qingdao Key Laboratory of Food Biotechnology,Qingdao 266404,China;Key Laboratory of Biological Processing of Aquatic Products,China National Light Industry,Qingdao 266404,China)

机构地区：[1]中国海洋大学食品科学与工程学院,海洋食品加工与安全控制全国重点实验室,山东青岛266404 [2]青岛海洋科技中心海洋药物与生物制品功能实验室,山东青岛266237 [3]青岛市食品生物技术重点实验室,山东青岛266404 [4]中国轻工业水产品生物加工重点实验室,山东青岛266404

出　　处：《中国海洋大学学报（自然科学版）》2024年第10期157-166,共10页Periodical of Ocean University of China

基　　金：国家自然科学基金项目(U21A20271);国家重点研究发展计划项目(2023YFD2401504);山东省重点研究发展计划项目(2022TZXD001);国家现代农业产业技术体系项目(CARS-48);青岛市市南区科技计划项目(2022-3-010-SW)资助。

摘　　要：为实现裂解性多糖单加氧酶(Lyticpolysaccharidemonooxygenase,LPMO)高效驱动甲壳素的降解,本文分析了来源于Oceanobacillussp.J11TS1的LPMO(OsLPMO10A)与甲壳素酶协同作用于不同晶型和不同致密性甲壳素的活性差异。研究表明,OsLPMO10A对β-甲壳素的结合活性和裂解作用比对α-甲壳素更强。采用一锅法反应,OsLPMO10A与甲壳素酶协同作用于β-甲壳素的协同度(2.41)和甲壳二糖产量((2.46±0.17)mg/mL)均高于协同作用于α-甲壳素的协同度(1.94)和甲壳二糖产量((0.68±0.04)mg/mL)。此外,虽然OsLPMO10A对致密性降低的α-甲壳素仍具有结合和氧化活性,但OsLPMO10A与甲壳素酶的协同度随着α-甲壳素致密性的降低而趋向于1。上述结果表明,甲壳素结构对LPMO驱动的甲壳素生物转化有重要影响。In order to achieve efficient biotransformation of chitin driven by a lytic polysaccharide monooxygenase(LPMO),the synergistic effect of LPMO(OsLPMO10A)from Oceanobacillus sp.J11TS1 and chitinases on different crystalline and different compactness chitin activities were analyzed.OsLPMO10A showed stronger binding and cleavage activities towardβ-chitin compared withα-chitin.Moreover,the degree of synergy(2.41)and the yield of chitobiose(GlcNAc)2((2.46±0.17)mg/mL)fromβ-chitin by one-pot enzymatic hydrolysis of OsLPMO10A and chitinase were higher than those ofα-chitin(1.94 and(0.68±0.04)mg/mL).Although OsLPMO10A still showed binding and oxidizing activities toward milledα-chitin with decreased compactness,the degree of synergy between OsLPMO10A and chitinases tended to be 1 with the reduction in compactness ofα-chitin.These results demonstrated that chitin structure plays an important role in the biotransformation of chitin driven by LPMO.

关 键 词：裂解性多糖单加氧酶 甲壳素酶 协同作用 α-甲壳素 甲壳寡糖 

分 类 号：Q814.9[生物学—生物工程]