The whole N fraction of six samples of hard and semi-hard pressed cheeses was analysed using PAGE, polyacrylanzide gel isoelectric focusing and immunoblotting with polyclonal antibodies against beta- and alpha(s1)-casein. The origin of some electrophoretic bands corresponding to peptides produced from the enzymic degradation of the casein fractions was established. A number of these peptides were also present in the in vitro hydrolysates of casein with plasmin and chymosin. Thus, it was also possible to determine which casein was the source of each peptide and which enzymes were active in cheese. Compared with the traditional Coomassie staining procedures, immunoblotting is more sensitive and specific, making the interpretation of each electrophoretic profile easy. Thus, it was also possible to obtain a clear picture of the state of each casein fraction in a cheese variety. Two main peptides were isolated from the pH 4.6-insoluble N fraction of Parmigiano-Reggiano using DEAE-cellulose chromatography and identified, from the amino acid sequence of the N- and C-terminal ends, as gamma(3)-casein ( (beta-casein(f108-209)) and alpha(s1)-PL1 (alpha(s1)-casein(f80-199). In both cases, a Lys-X bond was hydrolysed, indicating the action of a trypsin-like enzyme in beta- and alpha(s1)-casein hydrolysis during the ripening of this variety of hard pressed cheese.

GEL-ELECTROPHORESIS AND IMMUNOBLOTTING FOR THE DETECTION OF CASEIN PROTEOLYSIS IN CHEESE / F. ADDEO, G. GARRO, N. INTORCIA, L. PELLEGRINO, P. RESMINI, L. CHIANESE. - In: THE JOURNAL OF DAIRY RESEARCH. - ISSN 0022-0299. - 62:2(1995), pp. 297-309.

GEL-ELECTROPHORESIS AND IMMUNOBLOTTING FOR THE DETECTION OF CASEIN PROTEOLYSIS IN CHEESE

L. PELLEGRINO;P. RESMINI
Penultimo
;
1995

Abstract

The whole N fraction of six samples of hard and semi-hard pressed cheeses was analysed using PAGE, polyacrylanzide gel isoelectric focusing and immunoblotting with polyclonal antibodies against beta- and alpha(s1)-casein. The origin of some electrophoretic bands corresponding to peptides produced from the enzymic degradation of the casein fractions was established. A number of these peptides were also present in the in vitro hydrolysates of casein with plasmin and chymosin. Thus, it was also possible to determine which casein was the source of each peptide and which enzymes were active in cheese. Compared with the traditional Coomassie staining procedures, immunoblotting is more sensitive and specific, making the interpretation of each electrophoretic profile easy. Thus, it was also possible to obtain a clear picture of the state of each casein fraction in a cheese variety. Two main peptides were isolated from the pH 4.6-insoluble N fraction of Parmigiano-Reggiano using DEAE-cellulose chromatography and identified, from the amino acid sequence of the N- and C-terminal ends, as gamma(3)-casein ( (beta-casein(f108-209)) and alpha(s1)-PL1 (alpha(s1)-casein(f80-199). In both cases, a Lys-X bond was hydrolysed, indicating the action of a trypsin-like enzyme in beta- and alpha(s1)-casein hydrolysis during the ripening of this variety of hard pressed cheese.
Settore AGR/15 - Scienze e Tecnologie Alimentari
1995
Article (author)
File in questo prodotto:
Non ci sono file associati a questo prodotto.
Pubblicazioni consigliate

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/197499
Citazioni
  • ???jsp.display-item.citation.pmc??? 0
  • Scopus 54
  • ???jsp.display-item.citation.isi??? 44
social impact