MOE Key Laboratory of Marine Genetics and Breeding, College of Marine Life Sciences, Ocean University of China, Qingdao 266003, China.
Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266235, China.
Mar Drugs. 2020 Sep 16;18(9):466. doi: 10.3390/md18090466.
Endo-1,3-β-glucanases derived from marine mollusks have attracted much attention in recent years because of their unique transglycosylation activity. In this study, a novel endo-1,3-β-glucanase from the scallop , named L, was biochemically characterized. Unlike in earlier studies on marine mollusk endo-1,3-β-glucanases, L was expressed in vitro first. Enzymatic analysis demonstrated that L preferred to hydrolyze laminarihexaose than to hydrolyze laminarin. Furthermore, L was capable of catalyzing transglycosylation reactions with different kinds of glycosyl acceptors. More interestingly, the transglycosylation specificity of L was different from that of other marine mollusk endo-1,3-β-glucanases, although they share a high sequence identity. This study enhanced our understanding of the diverse enzymatic specificities of marine mollusk endo-1,3-β-glucanases, which facilitated development of a unique endo-1,3-β-glucanase tool in the synthesis of novel glycosides.
近年来，源于海洋贝类的内切-1,3-β-葡聚糖酶因其独特的转糖苷活性而备受关注。在这项研究中，我们对来自扇贝的一种新型内切-1,3-β-葡聚糖酶 L 进行了生化特性分析。与先前对海洋贝类内切-1,3-β-葡聚糖酶的研究不同，我们首先在体外表达了 L。酶学分析表明，L 更倾向于水解昆布六糖而非昆布聚糖。此外，L 能够催化不同糖基供体的转糖苷反应。更有趣的是，尽管 L 与其他海洋贝类内切-1,3-β-葡聚糖酶具有很高的序列同一性，但它们的转糖苷特异性却有所不同。这项研究增进了我们对内切-1,3-β-葡聚糖酶的酶学特异性的认识，这有助于开发独特的内切-1,3-β-葡聚糖酶工具，用于新型糖苷的合成。
