ISSN:
1432-0614
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Abstract A systematic study was made of the ability of aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2 to hydrolyse different peptide substrates. The enzyme showed a marked preference for sub-strates containing arginine as the N-terminal residue but, to a lesser extent, was also capable of cleaving other residues such as lysine and leucine. There was a tendency for the activity to increase with the hydrophobicity index of the C-terminal residue of dipeptide substrates. It was also observed that the enzyme tended to have higher affinities but lower V max values for tripeptides with hydrophobic C-terminal residues. The values determined for K m and V max increased with chain length for oligopeptides of the general formula Lys-Phe-(Gly) n , the optimum, as determined from V max/K m, being when n=4. Typical K m values for the most effective substrates were in the range 0.2–0.6 mM.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002530050526
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