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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
21/05/2024 |
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Data da última atualização: |
21/05/2024 |
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Autoria: |
GREEN, M. L.; FOSTER, P. M. D. |
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Afiliação: |
MARGARET L. GREEN. |
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Título: |
Comparison of the rates of proteolysis during ripening of Cheddar cheeses made with calf rennet and swine pepsin as coagulants. |
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Ano de publicação: |
1974 |
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Fonte/Imprenta: |
Journal of Dairy Research, v. 41, n. 2, p. 269-282, Jun. 1974. |
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DOI: |
https://doi.org/10.1017/S0022029900019683 |
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Idioma: |
Inglês |
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Conteúdo: |
The rates of proteolysis during ripening were followed in cheeses made with either calf rennet or swine pepsin and either starter or δ-gluconic acid lactone (GAL) as a replacement for the starter. A gel-filtration column technique and starch-gel electrophoresis were used for analysis, and bacterial counts were made on all samples. Proteolysis was faster in cheeses made using GAL than in those made using starter and also slightly faster in GAL cheeses made with swine pepsin than in those made with rennet. Further, it was considerably slower in starter-containing cheeses made with swine pepsin than in those made with rennet. It is suggested that these differences were due to the much greater rate of development of acidity in cheeses made with GAL than in those made with starter, which resulted in more of the coagulant being incorporated into the curd in an active state. The rate of proteolysis in starter-containing cheeses appeared to follow a characteristic course, being initially slow, then markedly increasing with a later slow decline. It is suggested that the increase in the rate of proteolysis was due to an increase in the total activity of bacterial proteinases released by lysis of the bacteria. Indications were obtained that the coagulants and bacterial proteinases catalysed broadly similar patterns of protein breakdown in cheese, and that medium-sized peptides (mol. wt 9000–14000) were formed as definite intermediates in the process. The results also showed that rennet and swine pepsin remained active for at least 7 months in GAL cheeses, that rennet contributed significantly to proteolysis in starter-containing cheeses, and that swine pepsin was at least extensively inactivated and possibly completely inactivated during cheese-making with starter. MenosThe rates of proteolysis during ripening were followed in cheeses made with either calf rennet or swine pepsin and either starter or δ-gluconic acid lactone (GAL) as a replacement for the starter. A gel-filtration column technique and starch-gel electrophoresis were used for analysis, and bacterial counts were made on all samples. Proteolysis was faster in cheeses made using GAL than in those made using starter and also slightly faster in GAL cheeses made with swine pepsin than in those made with rennet. Further, it was considerably slower in starter-containing cheeses made with swine pepsin than in those made with rennet. It is suggested that these differences were due to the much greater rate of development of acidity in cheeses made with GAL than in those made with starter, which resulted in more of the coagulant being incorporated into the curd in an active state. The rate of proteolysis in starter-containing cheeses appeared to follow a characteristic course, being initially slow, then markedly increasing with a later slow decline. It is suggested that the increase in the rate of proteolysis was due to an increase in the total activity of bacterial proteinases released by lysis of the bacteria. Indications were obtained that the coagulants and bacterial proteinases catalysed broadly similar patterns of protein breakdown in cheese, and that medium-sized peptides (mol. wt 9000–14000) were formed as definite intermediates in the process. The results also showed that rennet... Mostrar Tudo |
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Thesagro: |
Protease. |
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Thesaurus Nal: |
Cattle; Cheese milk; Cheeses; Proteolysis. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 02446naa a2200205 a 4500
001 2164366
005 2024-05-21
008 1974 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1017/S0022029900019683$2DOI
100 1 $aGREEN, M. L.
245 $aComparison of the rates of proteolysis during ripening of Cheddar cheeses made with calf rennet and swine pepsin as coagulants.$h[electronic resource]
260 $c1974
520 $aThe rates of proteolysis during ripening were followed in cheeses made with either calf rennet or swine pepsin and either starter or δ-gluconic acid lactone (GAL) as a replacement for the starter. A gel-filtration column technique and starch-gel electrophoresis were used for analysis, and bacterial counts were made on all samples. Proteolysis was faster in cheeses made using GAL than in those made using starter and also slightly faster in GAL cheeses made with swine pepsin than in those made with rennet. Further, it was considerably slower in starter-containing cheeses made with swine pepsin than in those made with rennet. It is suggested that these differences were due to the much greater rate of development of acidity in cheeses made with GAL than in those made with starter, which resulted in more of the coagulant being incorporated into the curd in an active state. The rate of proteolysis in starter-containing cheeses appeared to follow a characteristic course, being initially slow, then markedly increasing with a later slow decline. It is suggested that the increase in the rate of proteolysis was due to an increase in the total activity of bacterial proteinases released by lysis of the bacteria. Indications were obtained that the coagulants and bacterial proteinases catalysed broadly similar patterns of protein breakdown in cheese, and that medium-sized peptides (mol. wt 9000–14000) were formed as definite intermediates in the process. The results also showed that rennet and swine pepsin remained active for at least 7 months in GAL cheeses, that rennet contributed significantly to proteolysis in starter-containing cheeses, and that swine pepsin was at least extensively inactivated and possibly completely inactivated during cheese-making with starter.
650 $aCattle
650 $aCheese milk
650 $aCheeses
650 $aProteolysis
650 $aProtease
700 1 $aFOSTER, P. M. D.
773 $tJournal of Dairy Research$gv. 41, n. 2, p. 269-282, Jun. 1974.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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