期刊
BIOTECHNOLOGY LETTERS
卷 31, 期 6, 页码 883-887出版社
SPRINGER
DOI: 10.1007/s10529-009-9947-y
关键词
Biocatalyst; Bioconjugate; Enzyme modification; PEGylation; Protein stability
资金
- National Institute for General Medical Sciences (NIGMS) [S06 GM08102]
- NIH [R25 GM061151, T34 GM061151]
- Puerto Rico Development Company (PRIDCO)
alpha-Chymotrypsin was chemically modified with methoxypoly(ethylene glycol) (PEG) of different molecular weights (700, 2,000, and 5,000 Da) and the amount of polymer attached to the enzyme was varied systematically from 1 to 9 PEG molecules per enzyme molecule. Upon PEG conjugation, enzyme catalytic turnover (k (cat)) decreased by 50% and substrate affinity was lowered as evidenced by an increase in the K (M) from 0.05 to 0.19 mM. These effects were dependent on the amount of PEG bound to the enzyme but were independent of the PEG size. In contrast, stabilization toward thermal inactivation depended on the PEG molecular weight with conjugates with the larger PEGs being more stable.
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