@techreport{ee65069f5cdc45eeae7489685626abec,
title = "Proteolytic Activity of Three Generations of Fermentation-Produced Chymosin on Sodium Caseinate and During Cheddar Cheese Ripening",
abstract = "The proteolytic activities and specificities of three generations of fermentation-produced chymosin were investigated in cheese and in sodium caseinate (NaCN) digests made using these coagulants. The highest level of enzyme required to hydrolyse all intact αS1-CN in NaCN solution over 24 h was for modified camel chymosin (mCC), followed by camel chymosin (CC) and bovine chymosin (BC). Many peptides were separated and identified using liquid chromatography-mass spectrometry (LC-MS) from both Cheddar cheese and NaCN digests produced using each chymosin. In addition to previously reported major casein-derived peptides produced by bovine and camel chymosins and corresponding cleavage sites, several new cleavage sites were identified. The proteolytic specificity of mCC on casein was determined. Most of the peptides observed in Cheddar cheese samples were also identified in NaCN digests. The overall proteolytic activity of mCC was relatively lower than that of BC and CC, which may have implications for ripening and functionality of cheese.",
keywords = "Cheese, proteolysis, mass spectrometry, cheese ripening, enzymatic specificity, chymosin",
author = "Bozhao Li and McSweeney, \{Paul L.H.\} and Georg Arju and Anastassia Taivosalo and Taivo Lints and Tiina Kri{\v s}{\v c}iunaite and Raivo Vilu and John Lyne and Sebastien Roustel and Alan Kelly",
year = "2023",
month = jun,
day = "7",
doi = "10.2139/ssrn.4471940",
language = "English",
series = "INDA-D-23-00269",
type = "WorkingPaper",
}