Related Experiment Video
Updated: Aug 17, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Substrate specificity of the cell envelope-located proteinase of Lactococcus lactis subsp. lactis NCDO 763
V Monnet1, J P Ley, S Gonzàlez
1Station de Recherches Laitières, I.N.R.A. Jouy en josas, France.
Abstract:
1. The specificity of the cell envelope-located proteinase of Lactococcus lactis subsp. lactis NCDO 763 towards caseins has been submitted to a statistical study. Positive and negative relations have been evidenced between several amino acids and positions P6 to P'2 of the cleaved bonds. 2. Fragment 1-23 of alpha s1 and oxidized B chain of insulin are well cleaved by the proteinase while CMP (fragment 106-169 of kappa-casein) is a poor substrate. 3. Comparison with other cell envelope-located proteinase has been done. The enzyme of the strain 763 hydrolyses alpha s1-casein and fragment 1-23 of alpha s1-casein as the enzyme of the strain Sk11 and beta-casein as the enzyme of the strain Wg2. 4. The specificity of these proteinases and the comparison of their amino acid sequences let us postulate a more complex substrate binding area for these lactococcal proteinases than for the subtilisin.
More Related Videos
10:24Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii
Published on: April 10, 2020
05:58Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
Published on: February 24, 2026
Related Concept Videos
Operons
Lysosomal Hydrolases
Outer Layers of the Cell Envelope
Inducible Operons: lac Operon
Archaeal Cell Wall
Inhibitors of Gram-positive Cell Wall Synthesis