ESTERASE ACTIVITIES OF INDIGENOUS LACTIC ACID BACTERIA FROM ARGENTINEAN GOAT’S MILK AND CHEESES

OLISZEWSKI, R.; ROXANA MEDINA; GONZÁLEZ, S.N.; PÉREZ CHAIA, A.

Food Chemistry

Elsevier

Lugar: Holanda; Año: 2007 vol. 101 p. 1463 - 1467

0308-8146

Esterase activities of indigenous lactic acid bacteria isolated from goat’s milk and cheese were investigated. All the strains presented esterase activity on a-naphthyl derivative of fatty acids of 2 to 6 carbon atoms. L. fermentum ETC1 and L. bulgaricus ETC2 showed the highest specific activity on a-naphthyl acetate and L. rhamnosus ETC14 presented the highest specific acitivity on a-naphthyl butyrate and caproate. All enterococci strains presented the highest specific activities on a-naphthyl propionate, butyrate and caproate, and the lowest specific activities on a-naphthyl acetate. Pedicoccus pentosaseus ETC5 only had esterase activity on a-naphthyl acetate. The electrophoretic zymogram showed for each strain an individual enzyme profile on a-naphthyl acetate and revealed the presence of more than one esterase. L. plantarum ETC11 and E. faecium ETC9 presented four and five bands of esterase activity, respectively.  The strains evaluated in this work showed different esterase activity, which were species and strain specific.