Enzymatic characterization of Pseudomonas cepacia by API ZYM profile | Zendy

Chit Laa Poh | Zendy; Gunnar Loh | Zendy

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Enzymatic characterization of Pseudomonas cepacia by API ZYM profile

Author(s) -

Chit Laa Poh,

Gunnar Loh

Publication year - 1988

Publication title -

journal of clinical microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.349

H-Index - 255

eISSN - 1070-633X

pISSN - 0095-1137

DOI - 10.1128/jcm.26.3.607-608.1988

Subject(s) - esterase , pseudomonas , lipase , trypsin , biochemistry , microbiology and biotechnology , enzyme , valine , biology , chymotrypsin , pseudomonadaceae , amino acid , bacteria , genetics

The enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.

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