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Turkish Journal of Biology

DOI

10.3906/biy-0912-25

Abstract

A gene encoding \beta-(1,3-1,4)-glucanase (licA) was amplified from Orpinomyces sp. GMLF18 and expressed in Escherichia coli. The DNA sequence of licA showed that the gene was 707 bp and encoded a protein with a molecular mass of 26 kDa that belongs to family glycosyl hydrolase 16. The main LicA activity was observed to be cell-associated for the licA containing transformant E. coli, and the enzyme expressed in E. coli showed the highest activity at pH 5.0-6.0 and at temperatures of 40-50 °C. The enzyme was found to be stable at 40 °C; however, 12% of LicA activity was lost at 50 °C in 20 min. The licA was then introduced into the facultative anaerobic bacterium Lactococcus lactis subsp. cremoris MG1363 by a stable recombinant plasmid, pIL253. Although the enzymatic activity was lower than that in E. coli, the gene encoding the fungal originated lichenase was successfully expressed in L. lactis.

First Page

405

Last Page

414

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