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- W2108790439 abstract "ABSTRACT Optimization of immobilization process on crab shell chitosan was carried out. The chitosan purified from the crab shell was used as the matrix for the immobilization of α-galactosidase. The prepared matrix was activated with glutaraldehyde at different concentrations and different time intervals and coupling time was determined. Immobilization of α-galactosidase on crab shell chitosan resulted in 72% immobilization yield. The parameters like the effect of pH, temperature, thermal stability and storage stability were determined. The study revealed that immobilized enzyme shows better thermal and storage stability than the free enzyme. The performance of the free and immobilized α-galactosidase was tested in continuous stirred batch reactor to hydrolyze raffinose family oligosaccharides in soymilk. The oligosaccharide content of the soymilk was reduced by 77% in continuous reaction by immobilized α-galactosidase. PRACTICAL APPLICATIONS Chitosan used for the immobilization of α-galactosidase offers several advantages for enzyme immobilization and it contains all characteristic features for use as industrial material. Immobilization of one of the industrial important enzyme α-galactosidase, as it has many potential application in hydrolyzing raffinose series of oligosaccharides. The hydrolyzed soymilk after processing by immobilized α-galactosidase is free from flatus-inducing factors like raffinose and stachyose. It can be used as an alternative means for cow's milk for lactose intolerance, particularly among individuals in developing countries. As chitosan used is from the crustacean waste from the crab shell, the production and utilization of chitosan provides an economical alternative means of crustacean shell waste disposal sought worldwide." @default.
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- W2108790439 date "2008-08-01" @default.
- W2108790439 modified "2023-09-26" @default.
- W2108790439 title "OPTIMIZATION OF IMMOBILIZATION PROCESS ON CRAB SHELL CHITOSAN AND ITS APPLICATION IN FOOD PROCESSING" @default.
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- W2108790439 doi "https://doi.org/10.1111/j.1745-4514.2008.00182.x" @default.
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