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Title 

Adsorption immobilization of Escherichia coli phytase on probiotic Bacillus polyfermenticus spores

Authors 

E A ChoE J KimJae Gu Pan

Publisher 

Elsevier

Issue Date 

2011

Citation 

Enzyme and Microbial Technology, vol. 49, no. 1, pp. 66-71

Keywords 

Adsorption immobilizationBacillus sporeFeed enzymeGenerally recognized-as-safe (GRAS)PhytaseThermostability

Abstract 

The immobilization of enzymes on edible matrix supports is of great importance for developing stabilized feed enzymes. In this study, probiotic Bacillus spores were explored as a matrix for immobilizing Escherichia coli phytase, a feed enzyme releasing phosphate from phytate. Because Bacillus spore is inherently resistant to heat, solvents and drying, they were expected to be a unique matrix for enzyme immobilization. When mixed with food-grade Bacillus polyfermenticus spores, phytases were adsorbed to their surface and became immobilized. The amount of phytase attached was 28.2 ± 0.7 mg/g spores, corresponding to a calculated activity of 63,960 U/g spores; however, the measured activity was 41,120 ± 990.1 U/g spores, reflecting a loss of activity upon adsorption. Immobilization increased the half life (t1/2) of the enzyme three- to ten-fold at different temperatures ranging from 60 to 90 °C. Phytase was bound to the spore surface to the extent that ultrasonication treatment was not able to detach phytases from spores. Desorption of spore-immobilized phytase was only achieved by treatment with 1 M NaCl, 10% formic acid in 45% acetonitrile, SDS, or urea, suggesting that adsorption of phytase to the spore might be via hydrophobic and electrostatic interactions. We propose here that Bacillus spore is a novel immobilization matrix for enzymes that displays high binding capacity and provides food-grade safety.

ISSN 

0141-0229

Link 

http://dx.doi.org/10.1016/j.enzmictec.2011.03.006

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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