Characterization of fish myofibrillar protein by conjugation with alginate oligosaccharide prepared using genetic recombinant alginate lyase
Characterization of fish myofibrillar protein by conjugation with alginate oligosaccharide prepared using genetic recombinant alginate lyase
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DOI：
10.1111/j.1365-2621.2005.tb09021.x
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发表时间：
2005
影响因子：
3.9
通讯作者：
R. Sato;T. Sawabe;H. Saeki
中科院分区：
文献类型：
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作者：
R. Sato;T. Sawabe;H. Saeki
使用遗传修饰的大肠杆菌生产藻酸盐裂解酶在生产效率方面上级从埃氏假交替单胞菌的培养基中纯化藻酸盐裂解酶。当使用基因重组海藻酸裂解酶制备的海藻酸寡糖（AO）被引入到鱼肌原纤维蛋白，蛋白质获得高的水溶性和改善的热稳定性，类似于使用野生型裂解酶制备的AO。因此，利用基因重组技术生产海藻酸裂解酶将有助于通过与AO偶联来改善鱼类肌原纤维蛋白的功能。
: The production of alginate lyase using genetically modified Escherichia coli was superior to the purification of alginate lyase from a culture medium of Pseudoalteromonas elyakovii regarding production efficiency. When alginate oligosaccharide (AO) prepared using genetic recombinant alginate lyase was introduced to fish myofibrillar proteins, the protein obtained high water solubility and improved thermal stability, similarly to AO prepared using wild-type lyase. Therefore, the use of genetic recombinant technology for the production of alginate lyase would be useful for the functional improvement of fish myofibrillar proteins by conjugation with AO.