1999
DOI: 10.1080/08905439909549977
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Degradation of milk proteins by extracellular proteinase frombrevibacterium linensflk‐61

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Cited by 6 publications
(4 citation statements)
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“…β‐Casein was more rapidly hydrolyzed than α s1– casein in all cheeses (whereas degradation of α s1 ‐casein is faster than β‐casein in many cheeses). This greater degradation of β‐casein may be attributed to the higher pH of Halloumi cheese (pH ∼6.4–6.5), which favors the plasmin action (optimally active at pH ∼7.6) (Coskun and Sienkiewiez 1999; Sousa and McSweeney 2001). Compared with the other cheeses, e.g., Mozzarella (Dave et al.…”
Section: Resultsmentioning
confidence: 99%
“…β‐Casein was more rapidly hydrolyzed than α s1– casein in all cheeses (whereas degradation of α s1 ‐casein is faster than β‐casein in many cheeses). This greater degradation of β‐casein may be attributed to the higher pH of Halloumi cheese (pH ∼6.4–6.5), which favors the plasmin action (optimally active at pH ∼7.6) (Coskun and Sienkiewiez 1999; Sousa and McSweeney 2001). Compared with the other cheeses, e.g., Mozzarella (Dave et al.…”
Section: Resultsmentioning
confidence: 99%
“…The difference in rates of proteolysis between surface and core regions suggests that plasmin contributes more significantly to proteolysis in this cheese variety than chymosin. As well as well-characterised proteolytic pathways known to arise from the respective actions of these two enzymes, such as those leading to production of γ -caseins and α s1 -I-casein, enzymes of Brevibacterium linens are likely to have contributed to breakdown of both α s1 -and β-caseins [7,10]. Extracellular enzymes of B. linens have been reported to hydrolyse α s1 -casein more readily than β-casein [10] and to have alkaline pH optima [7], which would suggest that the surface of the cheese would exhibit significant α s1 -casein breakdown during ripening.…”
Section: Discussionmentioning
confidence: 99%
“…As well as well-characterised proteolytic pathways known to arise from the respective actions of these two enzymes, such as those leading to production of γ -caseins and α s1 -I-casein, enzymes of Brevibacterium linens are likely to have contributed to breakdown of both α s1 -and β-caseins [7,10]. Extracellular enzymes of B. linens have been reported to hydrolyse α s1 -casein more readily than β-casein [10] and to have alkaline pH optima [7], which would suggest that the surface of the cheese would exhibit significant α s1 -casein breakdown during ripening. However, this was not clearly evident, even in control cheese, suggesting that the relative importance of chymosin activity at the core was proportionately higher than that of extracellular proteinases at the surface.…”
Section: Discussionmentioning
confidence: 99%
“…At all ripening times, hydrolysis of a s1 -CN was more extensive in the surface layer compared to the core reflecting the contribution of the smear enzymes to hydrolysis, as the pH moved from the optimum value for chymosin activity (Fox, Law, McSweeney & Wallace, 1993;Fox & McSweeney, 1996). Enzymes from species present in the smear are known to hydrolyse a s1 -CN more readily than b-CN and to produce extracellular proteinases that have alkaline pH optima and, thus, may contribute to the enhanced hydrolysis at the surface of these types of cheese (Rattray, Fox, & Healy, 1996;Coskun & Sienkiewiez, 1999;Smacchi, Fox, & Gobbetti, 1999;Bikash, Ghosh, Sienkiwwicz & Krenkel, 2000). RP-HPLC peptide profiles of the 70% ethanol-soluble sub-fractions of pH 4.6-soluble extracts were performed throughout ripening for all cheese.…”
Section: Proteolysismentioning
confidence: 98%