Enzymatic activity and thermal stability of PEG-α-chymotrypsin conjugates

α-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 tu...

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Bibliographic Details
Published in:Biotechnology letters 2009-06, Vol.31 (6), p.883-887
Main Authors: Rodríguez-Martínez, José A., Rivera-Rivera, Izarys, Solá, Ricardo J., Griebenow, Kai
Format: Article
Language:English
Subjects:
Animals
Applied Microbiology
Biochemistry
Biological and medical sciences
Biomedical and Life Sciences
Biotechnology
Cattle
Chymotrypsin - chemistry
Chymotrypsin - metabolism
Enzyme Stability
Fundamental and applied biological sciences. Psychology
Kinetics
Life Sciences
Microbiology
Molecular Weight
Original Research Paper
Polyethylene Glycols - chemistry
Temperature
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Summary:α-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.
ISSN:0141-5492
1573-6776
DOI:10.1007/s10529-009-9947-y