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Molecules 2011, 16(12), 10046-10058; doi:10.3390/molecules161210046

Changes in Morphology and Activity of Transglutaminase Following Cross-Linking and Immobilization on a Polypropylene Microporous Membrane

1
Key Laboratory of Food Science and Engineering of Heilongjiang Province, Harbin University of Commerce, Harbin 150076, China
2
Harbin Hi-tech Soybean Food Co. Ltd., Harbin 150078, China
*
Author to whom correspondence should be addressed.
Received: 4 November 2011 / Revised: 28 November 2011 / Accepted: 30 November 2011 / Published: 5 December 2011
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Abstract

Transglutaminase (TGase) was cross-linked with glutaraldehyde, and cross-linked crystalline transglutaminase was immobilized on a polypropylene microporous membrane by UV-induced grafting. Immobilized enzyme activity were calculated to be 0.128 U/cm2 polypropylene microporous membrane. The microstructure and enzyme characteristics of free, cross-linked and immobilized transglutaminase were compared. The optimum temperature of free transglutaminase was determined to be approximately 40 °C, while cross-linking and immobilization resulted in an increase to approximately 45 °C and 50 °C. At 60 °C, immobilized, cross-linked and free transglutaminase retained 91.7 ± 1.20%, 63.2 ± 1.05% and 37.9 ± 0.98% maximum activity, respectively. The optimum pH was unaffected by the state of transglutaminase. However, the thermal and pH stabilities of cross-linked and immobilized transglutaminase were shown to increase.
Keywords: transglutaminase; cross-linking; immobilization; enzyme activity; microstructure transglutaminase; cross-linking; immobilization; enzyme activity; microstructure
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Shi, Y.-G.; Qian, L.; Zhang, N.; Han, C.-R.; Liu, Y.; Zhang, Y.-F.; Ma, Y.-Q. Changes in Morphology and Activity of Transglutaminase Following Cross-Linking and Immobilization on a Polypropylene Microporous Membrane. Molecules 2011, 16, 10046-10058.

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