CARACTERIZACIÓN DE AMINOPEPTIDASA N DE STREPTOCOCCUS THERMOPHILUS TW43
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| Format: | Artículo científico |
| Language: | es |
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Universidad Nacional de Misiones
2006
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| _version_ | 1876458874240761856 |
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| author | Emilio R. Marguet |
| author_facet | Emilio R. Marguet |
| contents | CARACTERIZACIÓN DE AMINOPEPTIDASA N DE STREPTOCOCCUS THERMOPHILUS TW43 Emilio R. Marguet Marisol Vallejo Micaela Pescuma Geología Aminopeptidase N Streptococcus thermophilus Biochemical and kinetic characteristics of the general Aminopeptidase N (PepN) from Streptococcus thermophilus TW43 were studied. Maximal activity of the enzyme was determined at pH 6.8 and 40ºC. Pep N was strongly inhibited by EDTA and o-phenanthroline. Therefore, it was considered to be a metallopeptidase. Imidazole partially inhibited enzyme activity suggesting histidine is one of the amino acids related to metal binding in the active site. Among the bivalent cations only Cu++ exhibited slight inhibition while Co++ increased enzymatic activity nearly fivefold. PepN remained active under ripening condition (pH 5.0 and 15ºC) suggesting that Streptococcus thermophilus TW43 may contribute to flavor cheese development through its role in production of free amino acids. 2006 artículo científico 0329-8922 https://www.redalyc.org/articulo.oa?id=382679020002 es http://www.redalyc.org/revista.oa?id=3826 Revista de Ciencia y Tecnología application/pdf Universidad Nacional de Misiones Revista de Ciencia y Tecnología (Argentina) Num.1 Vol.8 |
| format | Artículo científico |
| id | redalyc_382679020002 |
| institution | Redalyc |
| language | es |
| publishDate | 2006 |
| publisher | Universidad Nacional de Misiones |
| spellingShingle | CARACTERIZACIÓN DE AMINOPEPTIDASA N DE STREPTOCOCCUS THERMOPHILUS TW43 Emilio R. Marguet Geología Aminopeptidase N Streptococcus thermophilus CARACTERIZACIÓN DE AMINOPEPTIDASA N DE STREPTOCOCCUS THERMOPHILUS TW43 Emilio R. Marguet Marisol Vallejo Micaela Pescuma Geología Aminopeptidase N Streptococcus thermophilus Biochemical and kinetic characteristics of the general Aminopeptidase N (PepN) from Streptococcus thermophilus TW43 were studied. Maximal activity of the enzyme was determined at pH 6.8 and 40ºC. Pep N was strongly inhibited by EDTA and o-phenanthroline. Therefore, it was considered to be a metallopeptidase. Imidazole partially inhibited enzyme activity suggesting histidine is one of the amino acids related to metal binding in the active site. Among the bivalent cations only Cu++ exhibited slight inhibition while Co++ increased enzymatic activity nearly fivefold. PepN remained active under ripening condition (pH 5.0 and 15ºC) suggesting that Streptococcus thermophilus TW43 may contribute to flavor cheese development through its role in production of free amino acids. 2006 artículo científico 0329-8922 https://www.redalyc.org/articulo.oa?id=382679020002 es http://www.redalyc.org/revista.oa?id=3826 Revista de Ciencia y Tecnología application/pdf Universidad Nacional de Misiones Revista de Ciencia y Tecnología (Argentina) Num.1 Vol.8 |
| title | CARACTERIZACIÓN DE AMINOPEPTIDASA N DE STREPTOCOCCUS THERMOPHILUS TW43 |
| topic | Geología Aminopeptidase N Streptococcus thermophilus |
| url | https://www.redalyc.org/articulo.oa?id=382679020002 |