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Prolidase activity of Lactococcus lactis subsp. cremoris AM2: partial purification and characterization

Published online by Cambridge University Press:  01 June 2009

Mary Booth ,
Vincent Jennings ,
Ide Ní Fhaolain  and
Gerard O'Cuinn
Mary Booth
Affiliation:
Department of Biochemistry, University College Galway, Galway, Ireland
Vincent Jennings
Affiliation:
Department of Life Sciences, Regional Technical College, Galway, Ireland
Ide Ní Fhaolain
Affiliation:
Department of Life Sciences, Regional Technical College, Galway, Ireland
Gerard O'Cuinn
Affiliation:
Department of Life Sciences, Regional Technical College, Galway, Ireland
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Summary

Prolidase activity from cytoplasm of Lactococcus lactis subsp. cremoris (Streptococcus cremoris) AM2 was partially purified. The enzyme had Mr 42000 and optimum activity between pH 7·35 and 8·25 in citrate, phosphate and borate buffers while in a universal buffer system an optimum pH between 8·3 and 9·0 was observed. The activity was strongly inhibited by the chelating agents E.DTA, 1,10-phenanthroline and 8-hydroxyquinoline. Inhibition was also noted with dithio-threitol, N-ethylmaleimide and bacitracin. The enzyme was active on all amino-acylproline substrates tested except Gly-Pro and Gip-Pro and also showed activity against Pro-Pro. While most prolyl amino acids tested were not hydrolysed, hydrolysis was noted with Pro-Ala and Pro-Val. Km values of 20 mM and 10 mM were obtained with Phe-Pro and Met-Pro respectively; however, substrate inhibition was observed with Ile-Pro and Leu-Pro.

Type
Original Articles
Information
Journal of Dairy Research , Volume 57 , Issue 2 , May 1990 , pp. 245 - 254
Copyright
Copyright © Proprietors of Journal of Dairy Research 1990

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References

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