Caracterización de la inulinasa e invertasa en Candida utilis
lnvertase (E.C. 3.2.1.26) and inulinase (E.C. 3.2.1. 7) were analyzed in Candida utilis CECT 1061 to determine whether one single enzyme with both activities or two enzymes with different substrate specificities were present in this yeast. The synthesis of both fructofuranosidase activities was unde...
| Autores: | , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 1985 |
| País: | España |
| Institución: | Universidad de Murcia |
| Repositorio: | DIGITUM. Depósito Digital Institucional de la Universidad de Murcia |
| OAI Identifier: | oai:digitum.um.es:10201/1763 |
| Acceso en línea: | http://hdl.handle.net/10201/1763 |
| Access Level: | acceso abierto |
| Palabra clave: | Candida utilis Inulinasa Invertasa Enzimas CDU::5 - Ciencias puras y naturales::57 - Biología::577 - Bioquímica. Biología molecular. Biofísica |
| Sumario: | lnvertase (E.C. 3.2.1.26) and inulinase (E.C. 3.2.1. 7) were analyzed in Candida utilis CECT 1061 to determine whether one single enzyme with both activities or two enzymes with different substrate specificities were present in this yeast. The synthesis of both fructofuranosidase activities was under control of catabolite repression by glucose and they were present in whole cell extracts as well as in the extracellular culture fluids. The cell-associated activities appear mostly located in the periplasmic space. The two activities exhíbited an identical optimum pH and similar profiles of thermal denaturation. In addition, a constan! ratio was found between the inulinase and the invertase activities in a variety of culture condítions when extracellular media or cell extracts were assayed. From the results obtained it was concluded that both activities reside in a same protein of molecular weight close to 450,000 dalton which shows a different affiníty for sucrose and inuline, Km values were 14 and 0,62mM. respectively. |
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