Simultaneous purification and reversible immobilization of d-amino acid oxidase from Trigonopsis variabilis on a hydrophobic support |
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Authors: | Stanislaus F D’Souza Ashwini Deshpande |
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Institution: | (1) Nuclear Agriculture and Biotechnology Division, Bhabha Atomic Research Centre, 400085 Trombay, Mumbai, India |
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Abstract: | Purification and reversible immobilization of d-amino acid oxidase from Trigonopsis variabilis could be simultaneously accomplished by hydrophobic interaction on Phenyl Sepharose CL-4B in the presence of 50 mM pyrophosphate buffer (pH 8.5). The presence of a high salt concentration of 2M, which is generally required for the hydrophobic interactions, was not essential for the hydrophobic immobilization. The
enzyme in free as well as immobilized form was optimally active between pH 7.0 and 9.0. The immobilized preparation could
be reused in a batch process for the conversion of d-amino acids to α-keto acids. When the activity of the preparation dropped below practical limits, the gel could be regenerated
by water wash and recharged with fresh crude extract from yeast. |
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Keywords: | Immobilization Trigonopsis variabilis hydrophobic support Phenyl Sepharose CL-4B reversible immobilization α -keto acids d-amino acid oxidase" target="_blank">d-amino acid oxidase |
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