Biochemical Characterization of a Heat-Resistant κ-Carrageenase Capable of Tolerating High Temperatures up to 100 °C

文献类型： 外文期刊

第一作者： Jiang, Chengcheng

作者： Jiang, Chengcheng;Wang, Wei;Sun, Jingjing;Hao, Jianhua;Jiang, Chengcheng;Wang, Wei;Sun, Jingjing;Hao, Jianhua;Mao, Xiangzhao;Hao, Jianhua

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关键词： carrageenan; kappa-carrageenase; noncatalyticdomain; enzymatic properties

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.1； 五年影响因子：6.3 ）

ISSN： 0021-8561

年卷期： 2024 年

页码：

收录情况： SCI

摘要： kappa-Carrageenase plays a crucial role in the high-value utilization of carrageenan. Heat resistance is a key factor in the practical application of kappa-carrageenase, as carrageenan exhibits gel-like properties. Previous studies have shown that the C-terminal noncatalytic domains (nonCDs) can affect the thermostability of kappa-carrageenases. In this study, we expressed and characterized a kappa-carrageenase, MtKC16A, which contains three nonCDs, from Microbulbifer thermotolerans. MtKC16A has the highest activity at 80 degrees C and pH 7.0. Surprisingly, it exhibits excellent heat resistance, with 71.58% relative activity at 100 degrees C and still retains over 50% residual activity after incubation at 100 degrees C for 60 min. Additionally, MtKC16A has been shown to have a dual substrate hydrolysis activity. It can degrade kappa-carrageenan to produce highly single N kappa 4 and degrade beta/kappa-carrageenan to produce N kappa 2 and desulfated N kappa 4 DA-G-DA-G4S, suggesting its potential in producing kappa- and beta/kappa-hybrid oligosaccharides. Furthermore, we found that the unknown function domain (UNFD) in MtKC16A plays the most vital role among the three nonCDs. When this UNFD is truncated, the resulting mutants completely lose their catalytic ability at 100 degrees C. Finally, by introducing this UNFD to the C-terminal of another kappa-carrageenase CaKC16B, we were able to improve its heat resistance at 100 degrees C.

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