The enzymatic synthesis of β1-2 glucans
Incubation of labeled uridine diphosphate glucose with an enzyme preparation from Rhizobium meliloti or Agrobacterium tumefaciens leads to the formation of a glucan which appears to be identical to the β1-2 cyclic glucan described by several workers. This conclusion is based on the molecular size, t...
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| Autores principales: | , |
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1985
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v238_n2_p368_Zorreguieta http://hdl.handle.net/20.500.12110/paper_00039861_v238_n2_p368_Zorreguieta |
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| Sumario: | Incubation of labeled uridine diphosphate glucose with an enzyme preparation from Rhizobium meliloti or Agrobacterium tumefaciens leads to the formation of a glucan which appears to be identical to the β1-2 cyclic glucan described by several workers. This conclusion is based on the molecular size, the formation of sophorose and higher homologs by partial acid hydrolysis, the liberation of only glucose by total acid hydrolysis, and the release of only 3,4,6-tri-O-methylglucose after methylation and hydrolysis. A snail intestinal juice enzyme was found to break down the glucan and its partial hydrolysis products. A β-glucosidase from sweet almonds degraded sophorose but not the intact glucan. © 1985. |
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