Enzymatic activity and thermal stability of PEG-[alpha]-chymotrypsin conjugates
a-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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| Veröffentlicht in: | Biotechnology letters 2009-06, Vol.31 (6), p.883-887 |
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| container_title | Biotechnology letters |
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| creator | Rodriguez-Martinez, Jose A Rivera-Rivera, Izarys Sola, Ricardo J Griebenow, Kai |
| description | a-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. |
| doi_str_mv | 10.1007/s10529-009-9947-y |
| format | Article |
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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. 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| ispartof | Biotechnology letters, 2009-06, Vol.31 (6), p.883-887 |
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| language | eng |
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| source | SpringerLink Journals - AutoHoldings |
| subjects | Biochemistry Enzymatic activity Enzymes Inactivation Molecular weight Polyethylene glycol Polymers Proteins |
| title | Enzymatic activity and thermal stability of PEG-[alpha]-chymotrypsin conjugates |
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