ISSN:
0138-4988
Keywords:
Life Sciences
;
Life Sciences (general)
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Prolidase, a specific exopeptidase, is isolated from Escherichia coli B. The enzyme being present in the raw extract is purified and enriched by fractionated ammonium sulfate precipitation, ion exchange chromatography on DEAE-Sephadex A 50 as well as by gel filtration on Sepharose 4 B. Total yield of prolidase amounts to 19% with a 67fold enrichmentSubstrate specifity of the enzyme mainly corresponds to that of the animal prolidase. It is able to hydrolize the imido linkage at the N-terminal end of prolin in the case of di- and tripeptides. The temperature optimum of prolidase from E. coli B is 37 °C, the pH-optimum from pH 7.6 to 9.0. Storage stability at pH 8.6 and a temperature of 4 °C is optimal. The enzyme is only active in presence of Mn2+-ions. This metal cannot be replaced by Mg2-- or Zn2+-ionsA high enzyme activity and storage stability in presence of Mn2+-ions can be reached by immobilization of the prolidase, by covalent binding on Sepharose 6 B, adsorption on DEAE-Sephadex as well as by combination with glutar dialdehyde on DEAE-Sephadex.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/abio.370020208
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