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Applied and Environmental Microbiology, May 1999, p. 2035-2040, Vol. 65, No. 5
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cell-Wall-Bound Proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: Characterization and Specificity for beta -Casein

E. Tsakalidou,1,* R. Anastasiou,1 I. Vandenberghe,2 J. van Beeumen,2 and G. Kalantzopoulos1

Laboratory of Dairy Research, Department of Food Science and Technology, Agricultural University of Athens, 118 55 Athens, Greece,1 and Laboratory of Protein Biochemistry and Protein Engineering, University of Ghent, 9000 Ghent, Belgium2

Received 28 August 1998/Accepted 12 February 1999

Lactobacillus delbrueckii subsp. lactis ACA-DC 178, which was isolated from Greek Kasseri cheese, produces a cell-wall-bound proteinase. The proteinase was removed from the cell envelope by washing the cells with a Ca2+-free buffer. The crude proteinase extract shows its highest activity at pH 6.0 and 40°C. It is inhibited by phenylmethylsulfonyl fluoride, showing that the enzyme is a serine-type proteinase. Considering the substrate specificity, the enzyme is similar to the lactococcal PI-type proteinases, since it hydrolyzes beta -casein mainly and alpha - and kappa -caseins to a much lesser extent. The cell-wall-bound proteinase from L. delbrueckii subsp. lactis ACA-DC 178 liberates four main peptides from beta -casein, which have been identified.

* Corresponding author. Mailing address: Laboratory of Dairy Research, Agricultural University of Athens, Iera Odos 75, 118 55 Athens, Greece. Phone: 301.529-4676. Fax: 301.529-4672. E-mail: et{at}auadec.aua.gr.

Applied and Environmental Microbiology, May 1999, p. 2035-2040, Vol. 65, No. 5
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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