Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7599794 | Food Chemistry | 2014 | 6 Pages |
Abstract
The effect of succinimidyl carbonates activated methoxypolyethylene glycol (mPEG-SC) on the catalytic properties and conformation of native trypsin and dynamic high-pressure microfluidisation (DHPM) induced unfolded trypsin was studied. The thermal stability of unfolded trypsin was enhanced more significantly than that of native trypsin between 45 and 70 °C. The autolysis analysis indicated that modified unfolded trypsin was markedly more resistant to autolysis compared to modified native trypsin between 40 and 180 min. Upon mPEG-SC conjugation, the Km value of the enzyme decreased by about 2-fold, and the catalytic efficiency (Kcat/Km) increased by about 3-4-fold. Moreover, the increased thermal stability of unfolded trypsin might be due to the lower surface hydrophobicity and the higher hydrogen bond formation after mPEG-SC modification, which was reflected in the decrease of UV absorbance, the quenching and blue shift of fluorescence spectra, as well as the increase of β-sheet content.
Related Topics
Physical Sciences and Engineering
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Authors
Wei Liu, Jun-Ping Liu, Li-Qiang Zou, Zhao-Qin Zhang, Cheng-Mei Liu, Rui-Hong Liang, Ming-Yong Xie, Jie Wan,