Cellulose Acetate-polypropylene Composite Membrane Immobilized Phospholipase

doi:10.7506/spkx1002-6630-201309032

Abstract

Abstract:

The transglutaminase was immobilized on the cellulose acetate-polypropylene composite membrane in this study.
The activity of the enzyme was used as the index. Based on the single-factor tests, the effects of enzyme addition amount,
absorption time, glutaraldehyde concentration and glutaraldehyde cross-linking time on the activity of enzyme were studied.
The optimal immobilization conditions required enzyme concentration of 15 mg/mL, adsorption time of 3 h, glutaraldehyde
concentration of 0.3 g/100 mL, glutaraldehyde cross-linking time of 4 h. The activity of immobilized enzyme under the
optimal immobilization conditions was up to 16.1 U/g. The optimal temperature for the free enzyme was 35－40 ℃,
compared to 45－50 ℃ for the immobilized enzyme. The optimal pH for the free enzyme was 6－7, compared to pH 5－6
for the immobilized enzyme. Compared with the free enzyme, the immobilized enzyme was shifted to the acidity side.

Key words: cellulose acetate-polypropylene composite membrane, transglutaminase, enzyme activity, immobilization

CLC Number:

Q559.3

SHI Min，WANG Xue，MA Li-na，YU Dian-yu*. Cellulose Acetate-polypropylene Composite Membrane Immobilized Phospholipase[J]. FOOD SCIENCE, 2013, 34(9): 155-158.

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