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. 2013 Apr;26(4):552-7.
doi: 10.5713/ajas.2012.12557.

Immobilization of the Antarctic Bacillus sp. LX-1 α-Galactosidase on Eudragit L-100 for the Production of a Functional Feed Additive

Jaekoo Lee  1 , Inkyung Park  1 , Jaiesoon Cho  1
Affiliations

Immobilization of the Antarctic Bacillus sp. LX-1 α-Galactosidase on Eudragit L-100 for the Production of a Functional Feed Additive

Jaekoo Lee et al. Asian-Australas J Anim Sci. 2013 Apr.

Abstract

Partially purified α-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 α-galactosidase. The immobilized α-galactosidase was reutilized six times without significant loss in activity. The immobilized enzyme showed good storage stability at 37°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 α-galactosidase from Bacillus sp. LX-1 on Eudragit L-100 may be a promising strategy for removal of α-galacto-oligosaccharides such as raffinose and stachyose from soybean meal and other legume in feed industry.

Keywords: Bacillus; Eudragit L-100; Feed Industry; Immobilization; α-Galacto-oligosaccharides; α-Galactosidase.

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Figures

Figure 1.
Figure 1.
Immobilization of LX-1 α-galactosidase on Eudragit L-100. “A” represents the amount of enzyme theoretically bound to the matrix. This is calculated by subtracting the unbound activity in the supernatant from initially added enzyme. “B” represents the expressed activity of the particular immobilized preparation, measured after incubating the immobilized enzyme with the substrate. Data were expressed as mean±standard error from three experiments.
Figure 2.
Figure 2.
Zymogram analysis of α-galactosidase activity in the immobilized enzyme.
Figure 3.
Figure 3.
Reusability of the immobilized LX-1 α-galactosidase. Data were expressed as mean±standard error from three experiments.
Figure 4.
Figure 4.
Effect of pH on LX-1 α-galactosidase activity. Data were expressed as mean±standard error from three experiments. Immobilized enzyme (open circle with dotted line); free enzyme (closed circle with solid line).
Figure 5.
Figure 5.
Effect of temperature on LX-1 α-galactosidase activity. Data were expressed as mean±standard error from three experiments. Immobilized enzyme (open circle with dotted line); free enzyme (closed circle with solid line).
Figure 6.
Figure 6.
Storage stability of free and immobilized LX-1 α-galactosidase at 37°C. Data were expressed as mean±standard error from three experiments. Immobilized enzyme (open circle with dotted line); free enzyme (closed circle with solid line).
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