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Applied and Environmental Microbiology, December 2000, p. 5134-5140, Vol. 66, No. 12
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Autoproteolysis of Lactococcus lactis Lactocepin III Affects Its Specificity towards beta -Casein

Benedicte Flambard and Vincent Juillard*

Unité de Recherches Laitières et Génétique Appliquée, Institut National de la Recherche Agronomique, F-78350 Jouy-en-Josas, France

Received 22 May 2000/Accepted 13 September 2000

The effect of autoproteolysis of Lactococcus lactis lactocepin III on its specificity towards beta -casein was investigated. beta -Casein degradation was performed by using either an autolysin-defective derivative of L. lactis MG1363 carrying the proteinase genes of L. lactis SK11, which was unable to transport oligopeptides, or autoproteolyzed enzyme purified from L. lactis SK11. Comparison of the peptide pools by high-performance liquid chromatography analysis revealed significant differences. To analyze these differences in more detail, the peptides released by the cell-anchored proteinase were identified by on-line coupling of liquid chromatography to mass spectrometry. More than 100 oligopeptides were released from beta -casein by the cell-anchored proteinase. Analysis of the cleavage sites indicated that the specificity of peptide bond cleavage by the cell-anchored proteinase differed significantly from that of the autoproteolyzed enzyme.

* Corresponding author. Mailing address: Unité de Recherches Laitières et Génétique Appliquée, Institut National de la Recherche Agronomique, F-78350 Jouy-en-Josas, France. Phone: (33) 134 652 068. Fax: (33) 134 652 065. E-mail: juillard{at}jouy.inra.fr.

Applied and Environmental Microbiology, December 2000, p. 5134-5140, Vol. 66, No. 12
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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