Abstract
In this work, peptidases of four yeast species frequently encountered in dairy products, i.e. Kluyveromyces lactis, Saccharomyces cerevisiae, Debaryomyces hansenii and Pichia anomala, were investigated with respect to activity towards β-casein-derived peptides and compared with the activity of six bacterial species, i.e. Lactobacillus helveticus, Lactobacillus plantarum, Leuconostoc lactis, Pediococcus pentosaceus, Bifidobacterium bifidum and Brevibacterium linens. Cell-free extracts (CFE) obtained by mechanical disruption were standardised in terms of protein content, then added to a β-casein hydrolysate. The free amino acid release at 24°C and pH 5.7 was monitored over a period of 168 h. Free amino acid and peptide profiles were determined by chromatography. The yeasts tested exhibited a higher peptidase activity than all bacterial species except Lb. helveticus, which had comparable activity. Yeast CFE were less efficient in proline release compared with Lb. helveticus, but more efficient at degrading β-casein putative phosphorylated peptides. These results support the proposition that yeasts can significantly influence proteolysis in cheese.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
