Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, 600 S. Mathews Ave, Urbana, IL, 61801, USA.
Genetic Engineering and Biotechnology Research Institute, University of Sadat City, El Sadat City, Egypt.
Appl Microbiol Biotechnol. 2020 Jan;104(1):161-171. doi: 10.1007/s00253-019-10243-0. Epub 2019 Nov 21.
Laminarin is an abundant glucose polymer used as an energy reserve by micro- and macroalgae. Bacteria digest and consume laminarin with laminarinases. Their genomes frequently contain multiple homologs; however, the biological role for this replication remains unclear. We investigated the four laminarinases of glycoside hydrolase families GH16 and GH17 from the marine bacterium Vibrio breoganii 1C10, which can use laminarin as its sole carbon source. All four laminarinases employ an endolytic mechanism and specifically cleave the β-1,3-glycosidic bond. Two primarily produce low-molecular weight laminarin oligomers (DP 3-4) whereas the others primarily produce high-molecular weight oligomers (DP > 8), which suggests that these enzymes sequentially degrade laminarin. The results from this work provide an overview of the laminarinases from a single marine bacterium and also provide insights regarding how multiple laminarinases are used to degrade laminarin.
昆布多糖是一种丰富的葡萄糖聚合物，被微藻和海藻用作能量储备。细菌用昆布多糖酶消化和消耗昆布多糖。它们的基因组经常包含多个同源物；然而，这种复制的生物学作用尚不清楚。我们研究了海洋细菌 Vibrio breoganii 1C10 的糖苷水解酶家族 GH16 和 GH17 的四种昆布多糖酶，它们可以将昆布多糖作为唯一的碳源。这四种昆布多糖酶都采用内切机制，专门切割β-1,3-糖苷键。两种酶主要产生低分子量的昆布多糖低聚物（DP 3-4），而其他酶主要产生高分子量的低聚物（DP > 8），这表明这些酶依次降解昆布多糖。这项工作的结果提供了来自单个海洋细菌的昆布多糖酶的概述，也提供了关于如何使用多种昆布多糖酶来降解昆布多糖的见解。
