Abstract
Soy protein isolate (SPI) construction enabled it to covalently conjugate β-d-galactosidase (βGL) to κ-Carrageenan (Car) hydrogel beads following a glutaraldehyde (GA) processing step. The utilization of a 10% (w/w) SPI at pH 5 and a 25% (v/v) GA solution was shown to be optimal for processing the Car beads in order to provide the loftiest quantity of immobilized βGL (iβGL). The effect of the loading βGL activity was also investigated, and it was unveiled that a 96.45% immobilization efficiency could be achieved if the processed Car beads were loaded with 6.78 Ug−1 βGL. The processed Car beads were characterized via EDX and SEM. Furthermore, the pH profiles, the temperature profiles and the activation energies for lactose hydrolysis were investigated for the free and the processed Car iβGLs. Additionally, the iβGL operational stability was studied, and it was unveiled that the iβGL offered 83.37 ± 3.39% of its commencing activity during the 12th catalytic cycle.
Published Version
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