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首页> 外文期刊>Frontiers in Bioengineering and Biotechnology >Characterization of a Novel α-Neoagarobiose Hydrolase Capable of Preparation of Medium- and Long-Chain Agarooligosaccharides
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Characterization of a Novel α-Neoagarobiose Hydrolase Capable of Preparation of Medium- and Long-Chain Agarooligosaccharides

机译:一种新型α-新蛋白酶水解酶的表征能够制备中链和长链琼脂糖糖苷

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α-Neoagarobiose hydrolase plays an important role in saccharification processes of marine biomass. In this study, a α-neoagarobiose hydrolase from Streptomyces coelicolor A3(2), designated as ScJC117, was identified, purified and characterized. It has a sequence of 370 amino acids and belongs to the GH117 family. ScJC117 exhibited good activity under optimal hydrolysis conditions of pH 6.0 and 30°C, where it showed the Km and kcat for neoagarobiose of 11.57 mM and 0.48 s-1, respectively. ScJC117 showed the ability to hydrolyze neoagarooligosaccharides with the polymerization degrees of 2-14. Basis of catalytic activity toward the first α-1,3-glycosidic bond of the neoagarooligosaccharides from the non-reducing end, ScJC117 can be classified as an exo-type α-neoagarobiose hydrolase. These results suggested that ScJC117 could be used in the preparation of odd agarooligosaccharides (especially agaroheptaose-agaroundecaose) and 3, 6-anhydro-L-galactose, which has as functional food additive potential. Moreover, ScJC117 can be used for comprehensive utilization of red algae.
机译:α-新加药水解酶在海洋生物质的糖化过程中起着重要作用。在该研究中,鉴定了指定为SCJC117的链霉菌的α-新加药水解酶,其被称为SCJC117,纯化和表征。它具有370个氨基酸的序列,属于GH117家族。 SCJC117在pH6.0和30℃的最佳水解条件下表现出良好的活性,其中分别显示了11.57mm和0.48s-1的新蛋白酶的KM和Kcat。 SCJC117显示了使用2-14的聚合度水解新卤代乳糖苷的能力。催化活性朝向来自非还原末端的新卤代酚的第一α-1,3-糖苷键的基础,SCJC117可以分类为EXO型α-新蛋白酶水解酶。这些结果表明SCJC117可用于制备奇琼脂糖核苷酸(特别是Agaroheptaose-agaroundEcaose)和3,6-α-溶胶半乳糖,其具有作为功能性食品添加剂潜力的。此外,SCJC117可用于综合利用红藻。

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