Biochemical Characterization of a Cold-Adapted λ-Carrageenase OUC-CglA from Maribacter vaceletii : An Efficient Tool for λ-Carrageenan Degradation

作者：Zewei Lu, Hong Jiang, Hamed I. Hamouda, Tao Wang, Yueyang Dong, Xiangzhao Mao · 发表于：Journal of Agricultural and Food Chemistry · 年份：2022 · DOI：10.1021/acs.jafc.2c05544 · 被引用次数：10 · 研究领域：Seaweed-derived Bioactive Compounds、Enzyme Production and Characterization、Protein Hydrolysis and Bioactive Peptides

λ-Carrageenase with high activity is an effective and environmentally friendly tool enzyme for the preparation of λ-carrageenan oligosaccharides with various biological activities. Herein, a novel GH150 (glycoside hydrolases family 150) λ-carrageenase OUC-CglA from Maribacter vaceletii was heterologously expressed, purified, and characterized. The recombinant OUC-CglA performs strict selectivity toward λ-carrageenan with a specific activity of 418.7 U/mg under its optimal reaction conditions of 20 °C and pH 7.0. Additionally, OUC-CglA is a typical cold-adapted λ-carrageenase because it unfolds 90% and 63% of its maximum activity at 15 and 10 °C, respectively. The hydrolysis process suggests that OUC-CglA is an endotype λ-carrageenase with the final products consisting of λ-neocarrabiose, λ-neocarratetraose, λ-neocarrahexaose, and other long-chain λ-neocarrageenan oligosaccharides. As a result, high activity, cold-adaptation, and principal products of OUC-CglA make it a potential biocatalyst for the effective preparation of λ-carrageenan oligosaccharides.