Stabilization of beta-Galactosidase Encapsulated in Pectin-Alginate Hydrogel and Hydrolysis of Whey Lactose and Whole Milk

JOURNAL OF THE BRAZILIAN CHEMICAL SOCIETY(2023)

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Abstract
The operational conditions of 0-galactosidase encapsulated in pectin-alginate hydrogel were investigated as well as its catalytic activity in the hydrolysis of lactose from whey and whole milk. 0-Galactosidase encapsulated in pectin-alginate hydrogel showed the best results to yields and diffusional effect and pH range. Thermostability showed considerable income gain for half-life (1.7-fold), activation energy of denaturation (31.6-fold), activation of denaturation (217.3-fold at 40 degrees C; 266.8-fold at 50 degrees C; 345.6-fold at 60 degrees C), and entropy of activation of denaturation (-42.0 J mol-1 K-1). Reusability of encapsulated 0-galactosidase was observed in 8-cycles for the milk whey lactose hydrolysis (51.9%) and 7-cycles for whole milk (55.6%), and the lactose hydrolysis was observed in 13% in milk whey and 10.3% in whole milk after 10 cycles. These results revealed an industrial application potential of 0-galactosidase encapsulated in pectin-alginate hydrogel for lactose hydrolysis of milk whey and whole milk processes.
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Key words
enzyme encapsulation, lactase, thermostability, reusability, lactose hydrolysis
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