Abstract
ABSTRACT: Polymerization by microbial transglutaminase (mTGase) of disulfide bond‐cleaved bovine serum albumin treated with 2‐mercaptoethanol was investigated in an oil‐in‐water model emulsion system. Fluorescence and circular dichroism spectroscopy revealed that conformational changes in tertiary structure were more distinct as compared with the secondary structure. Reduced protein was polymerized more effectively by mTGase. Highest storage modulus was observed in the emulsion gel formed by both 2‐ME and mTGase treatments. The phase angle was less than 45° in all samples with 2‐ME and enzyme treatments, an indication that the conformational changes due to the reduction and polymerization contribute significantly to the formation of emulsion gels.
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