Premium
Diversity in specificity of the extracellular proteinases in Lactobacillus helveticus and Lactobacillus delbrueckii subsp. bulgaricus
Author(s) -
Oberg C.J.,
Broadbent J.R.,
Strickland M.,
McMahon D.J.
Publication year - 2002
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1472-765x.2002.01123.x
Subject(s) - lactobacillus , lactobacillus helveticus , lactobacillus delbrueckii subsp. bulgaricus , biology , lactobacillaceae , microbiology and biotechnology , extracellular , diversity (politics) , bacteria , genetics , sociology , anthropology
Aims: To investigate the diversity in specificity of cell‐bound extracellular proteinases in Lactobacillus helveticus and Lactobacillus delbrueckii subsp. bulgaricus . Methods and Results: HPLC analysis of whole‐cell preparations of 14 Lact. delbrueckii subsp. bulgaricus and eight Lact. helveticus strains incubated with α s1 ‐casein (f 1–23) detected at least six distinct proteolytic patterns. Differences between groups were found in both the primary and secondary specificity toward α s1 ‐casein (f 1–23) and its breakdown products. No correlation was found between the o ‐phthaldialdehyde (OPA) general proteolysis analysis and α s1 ‐casein (f 1–23) cleavage profiles. Conclusions, Significance and Impact of Study: Using the α s1 ‐CN (f 1–23) method, six patterns of proteolysis were found in the dairy lactobacilli tested. Understanding the influence of Lactobacillus proteinase specificity on casein degradation should facilitate efforts to develop starter cultures that predictably improve the functional properties of Mozzarella cheese.