2004
DOI: 10.1016/s1874-558x(04)80076-9
|View full text |Cite
|
Sign up to set email alerts
|

Proteolysis in Cheese during Ripening

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

0
150
0
10

Year Published

2006
2006
2016
2016

Publication Types

Select...
5
4

Relationship

0
9

Authors

Journals

citations
Cited by 145 publications
(160 citation statements)
references
References 301 publications
0
150
0
10
Order By: Relevance
“…Proteolysis, which contributes to the development of cheese texture and flavor, is due to the action of enzymes from (a) coagulant, (b) milk (general plasmin), (c) starter bacteria, (d) the adventitious nonstarter microflora and (e) secondary starter (in some cheese varieties). The proteolytic system of lactic acid bacteria (LAB) consists of proteinases, which hydrolyze caseins, and large peptides and peptidases, which are responsible for the liberation of small peptides and free amino acids (FAA), an essential step in cheese ripening [43].…”
Section: Introductionmentioning
confidence: 99%
“…Proteolysis, which contributes to the development of cheese texture and flavor, is due to the action of enzymes from (a) coagulant, (b) milk (general plasmin), (c) starter bacteria, (d) the adventitious nonstarter microflora and (e) secondary starter (in some cheese varieties). The proteolytic system of lactic acid bacteria (LAB) consists of proteinases, which hydrolyze caseins, and large peptides and peptidases, which are responsible for the liberation of small peptides and free amino acids (FAA), an essential step in cheese ripening [43].…”
Section: Introductionmentioning
confidence: 99%
“…The presence of cathepsins D (EC 3.4.23.5) and B (EC 3.4.22.1) in milk was confirmed (Upadhyay et al 2004).…”
mentioning
confidence: 84%
“…In milk, plasminogen, plasmin and plasminogen activators are associated with the casein micelles while plasmin inhibitors and inhibitors of plasminogen activators are in the serum phase. Plasmin has trypsin-like specificity and acts on caseins in the order β ≈ α s2 >> α s1 , while κ-casein appears to be resistant (Upadhyay et al 2004). Although optimal conditions for plasmin activity are about 37°C and pH 7.5, it can evoke proteolytic changes during raw milk storage at 4°C, as well ).…”
mentioning
confidence: 99%
“…The lower pH in trial cheeses could also explain similar proteolysis observed in control and trial cheeses despite their differences in moisture content. Indeed, primary proteolysis is well known to be enhanced by higher moisture content but decreased by lower pH [20].…”
Section: Composition Of the Ripened Cheesesmentioning
confidence: 99%