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FRI researchers build novel α-galactosidase resources
α-Galactosidase has the hydrolysis ability to catalyze the breakage of α-D-galactoside bond and transglycosylation activity, and it is widely used in the feed, medicine, food and chemical industries. To alleviate the anti-nutritional effect of galactooligosaccharides (GOS) in soybean meal and promote animal health, α-galactosidase is generally supplemented in the feed stuff. Due to the high cost, low yield, and the rmoliability under high-temperature feed processing conditions limited the application of α-galactosidase.
Dr. Yao bin, senior scientist of Feed Research Institute (FRI), Chinese academy of agricultural sciences (CAAS), led the enzymetic engineering research team to work on α-galactosidase and to clone novel α-galactosidase genes from the rmophilic microorganisms, to construct high-yield secretory engineering strains, and to provide cost-effective α-galactosidase candidates with excellent properties and high productivity for potential industrial application.
By the enzyme protein purification and gene cloning, six novel α-galactosidases from the rmophilic microorganisms were obtained with potential application. And, two different structure GH27 α-galactosidases degradation on guar galactomannan with different degrees of galactose substitution (21- 38%) and konjac galactomannan, was studied and laying the foundation for substrate specificity of GH27 α-galactosidase , enriching the α-galactosidase genetic resources, and providing a good materials for research and industrial applications.
The research has been published in The Bioresource Technology. More details are available the links bellow:
http://www.sciencedirect.com/science/article/pii/s096085241301804X.

Dr. Yao bin, senior scientist of Feed Research Institute (FRI), Chinese academy of agricultural sciences (CAAS), led the enzymetic engineering research team to work on α-galactosidase and to clone novel α-galactosidase genes from the rmophilic microorganisms, to construct high-yield secretory engineering strains, and to provide cost-effective α-galactosidase candidates with excellent properties and high productivity for potential industrial application.

By the enzyme protein purification and gene cloning, six novel α-galactosidases from the rmophilic microorganisms were obtained with potential application. And, two different structure GH27 α-galactosidases degradation on guar galactomannan with different degrees of galactose substitution (21- 38%) and konjac galactomannan, was studied and laying the foundation for substrate specificity of GH27 α-galactosidase , enriching the α-galactosidase genetic resources, and providing a good materials for research and industrial applications.
The research has been published in The Bioresource Technology. More details are available the links bellow:
http://www.sciencedirect.com/science/article/pii/s096085241301804X.
By Wang Yuan
Wangyuan08@caas.cn
Wangyuan08@caas.cn
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