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Comparative Study on Enzymatic Characteristics of Two κ-Carrageenases from Carrageenan-Degrading Bacterium Catenovulum agarivorans DS2

文献类型： 外文期刊

作者： Jiang, Chengcheng 1 ; Wang, Wei 1 ; Sun, Jingjing 1 ; Hao, Jianhua 1 ; Mao, Xiangzhao 2 ;

作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, State Key Lab Mariculture Biobreeding & Sustainabl, Lab Marine Drugs & Byproducts,Natl Lab Marine Sci, Qingdao 266071, Peoples R China

2.Ocean Univ China, Coll Food Sci & Engn, Qingdao 266003, Peoples R China

3.Jiangsu Collaborat Innovat Ctr Exploitat & Utiliza, Lianyungang 222005, Peoples R China

关键词： kappa-carrageenase; noncatalytic domain; enzymatic property; metabolic pathway

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 72 卷 22 期

页码：

收录情况： SCI

摘要： kappa-Carrageenase plays an important role in achieving the high-value utilization of carrageenan. Factors such as the reaction temperature, thermal stability, catalytic efficiency, and product composition are key considerations for its large-scale application. Previous studies have shown that the C-terminal noncatalytic domains (nonCDs) could influence the enzymatic properties, of kappa-carrageenases, providing a strategy for exploring kappa-carrageenases with different properties, especially catalytic products. Accordingly, two kappa-carrageenases (CaKC16A and CaKC16B), from the Catenovulum agarivorans DS2, were selected and further characterized. Bioinformatics analysis suggested that CaKC16A contained a nonCD but CaKC16B did not. CaKC16A exhibited better enzymatic properties than CaKC16B, including thermal stability, substrate affinity, and catalytic efficiency. After truncation of the nonCD of CaKC16A, its thermal stability, substrate affinity, and catalytic efficiency have significantly decreased, indicating the vital role of nonCD in maintaining a good enzymatic property. Moreover, CaKC16A degraded kappa-carrageenan to produce a highly single kappa-neocarratetrose, while CaKC16B produced a single kappa-neocarrabiose. CaKC16A could degrade beta/kappa-carrageenan to produce a highly single desulfated kappa-neocarrahexaose, while CaKC16B produced kappa-neocarrabiose and desulfated kappa-neocarratetrose. Furthermore, it was proposed that CaKC16A and CaKC16B participate in the B/KC metabolic pathway and serve different roles, providing new insight into obtaining kappa-carrageenases with different properties.

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