These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Cell-wall-associated proteinase of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397: differential extraction, purification and properties of the enzyme.
    Author: Laloi P, Atlan D, Blanc B, Gilbert C, Portalier R.
    Journal: Appl Microbiol Biotechnol; 1991 Nov; 36(2):196-204. PubMed ID: 1368107.
    Abstract:
    Whole cells of Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 were able to hydrolyse alpha- and beta-caseins. Irrespective of the growth medium used, milk or De Man-Rogosa-Sharpe (MRS) broth, identical patterns of alpha- and beta-casein hydrolytic products, respectively, were visualized by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. A soluble proteinase present in cell-wall extracts was active on caseins and displayed the same hydrolytic patterns as whole cells. It was purified from cell-wall extract to homogeneity by ultrafiltration and ion exchange chromatography. The enzyme is a monomer with a molecular mass of 170 kDa, an optimum temperature of 42 degrees C and an optimum pH of 5.5. It was strongly activated by dithiothreitol and partially inhibited by E-64. These properties indicate that cysteine residues play an important role in the enzyme mechanism. The purified proteinase was not able to hydrolyse di- or tripeptides.
    [Abstract] [Full Text] [Related] [New Search]