The aim of this study was to compare the proteolytic activity by incubating whole ovine casein with 6 industrial (liquid and paste) and two traditional (paste) rennet preparations from calf, lamb and kid. Casein hydrolysate was analysed by pH 8.6 urea-PAGE analysis and immunoblotting using polyclonal antibodies against αs1 and β-casein (CN). The degradation patterns showed that αs1-CN was hydrolysed more quickly than β-CN giving rise to αs1-I casein. The highest degree of proteolysis was observed in 3 types of industrial rennet, two from lamb, either liquid or paste, and one liquid from calf. Rennet from kid (industrial or traditional/liquid or paste) showed the lowest proteolytic activity. The pepsin content was very different among the tested rennet samples, probably explaining the difference in proteolytic activity.
Proteolytic activities of animal rennet on ovine casein / Papoff, C. M.; Mauriello, Rosalba; Pirisi, A.; Piredda, G.; Addis, M.; Chianese, Lina. - In: MILCHWISSENSCHAFT. - ISSN 0026-3788. - STAMPA. - 59 (7/8):(2004), pp. 414-417.
Proteolytic activities of animal rennet on ovine casein
MAURIELLO, ROSALBA;CHIANESE, LINA
2004
Abstract
The aim of this study was to compare the proteolytic activity by incubating whole ovine casein with 6 industrial (liquid and paste) and two traditional (paste) rennet preparations from calf, lamb and kid. Casein hydrolysate was analysed by pH 8.6 urea-PAGE analysis and immunoblotting using polyclonal antibodies against αs1 and β-casein (CN). The degradation patterns showed that αs1-CN was hydrolysed more quickly than β-CN giving rise to αs1-I casein. The highest degree of proteolysis was observed in 3 types of industrial rennet, two from lamb, either liquid or paste, and one liquid from calf. Rennet from kid (industrial or traditional/liquid or paste) showed the lowest proteolytic activity. The pepsin content was very different among the tested rennet samples, probably explaining the difference in proteolytic activity.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.