Asian-Australasian Journal of Animal Sciences

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
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Immobilization of the Antarctic Bacillus sp. LX-1 α-Galactosidase on Eudragit L-100 for the Production of a Functional Feed Additive

  • Lee, Jaekoo (Department of Animal Sciences and Environment, College of Animal Bioscience and Technology, Konkuk University) ;
  • Park, Inkyung (Department of Animal Sciences and Environment, College of Animal Bioscience and Technology, Konkuk University) ;
  • Cho, Jaiesoon (Department of Animal Sciences and Environment, College of Animal Bioscience and Technology, Konkuk University)
  • Received : 2012.10.09
  • Accepted : 2012.12.02
  • Published : 2013.04.01
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Abstract

Partially purified ${\alpha}$-galactosidase from Bacillus sp. LX-1 was non-covalently immobilized on a reversibly soluble-insoluble polymer, Eudragit L-100, and an immobilization efficiency of 0.93 was obtained. The optimum pH of the free and immobilized enzyme was 6.5 to 7.0 and 7.0, respectively, while there was no change in optimum temperature between the free and immobilized ${\alpha}$-galactosidase. The immobilized ${\alpha}$-galactosidase was reutilized six times without significant loss in activity. The immobilized enzyme showed good storage stability at $37^{\circ}C$, retaining about 50% of its initial activity even after 18 d at this temperature, while the free enzyme was completely inactivated. The immobilization of ${\alpha}$-galactosidase from Bacillus sp. LX-1 on Eudragit L-100 may be a promising strategy for removal of ${\alpha}$-galacto-oligosaccharides such as raffinose and stachyose from soybean meal and other legume in feed industry.

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References

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