Coconut α-d-galactosidase isoenzymes: isolation, purification and characterization

Abstract

α-d-Galactosidases (α-d-galactoside galactohydrolase, EC 3.2.1.22) from normal coconut endosperm were isolated and partially purified by a combination of ammonium sulfate fractionation, SP-Sephadex C50-120 ion-exchange chromatography and Sephadex G-200 and G-100 gel filtration. Two molecular forms of the enzyme, designated as A and B, were eluted after SP-Sephadex C50-120 ion-exchange chromatography. α-d-Galactosidase A, which is the major isoenzyme, was partially purified 43-fold on Sephadex G-200 and has a MW of about 23 000 whereas α-d-galactosidase B was partially purified 23-fold on Sephadex G-100 and has a similar MW of about 26 600. Both isoenzymes exhibited optimum activity at pH 7.5. The apparent Km and Vmax of α-d-galactosidase A were obtained at 3.46 × 10-4M and 1.38 × 10-3 M p-nitrophenyl α-

Source or Periodical Title

Phytochemistry

ISSN

319422

Page

1251-1254

Document Type

Article

Subject

coconut, Cocos nucifera, enzyme purification, mutant endosperm., Palmae, regulation, α-d-galactosidase

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