ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Pyridoxaminephosphate oxidase (EC 1.4.3.5, deaminating) that was partially purified about 40-fold from dry baker's yeast was immobilized to iodo- and bromoacetyl polysaccharides. The most effective carrier was an iodoacetyl cellulose, to which almost complete activity of pyridoxine 5′-phosphate oxidase was immobilized in 0.02M potassium phosphate buffer (pH 8.5) containing 2M ammonium sulfate at 4°C. The immobilized enzyme was more stable than the purified, soluble enzyme against heat and pH change. It was confirmed that N-(5′-phosphopyridoxyl)-L-serine was degradedly oxidized to pyridoxal 5′-phosphate and L-serine by the immobilized enzyme as comparable rate as pyridoxine 5′-phosphate, whereas N-(5′-phosphopyridoxyl)-D-serine did not serve as substrate, as in the purified, soluble enzyme.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260260503
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