Purification and properties of alpha-galactosidase from white-rot fungus Pleurotus florida.

Simple item page
dc.contributor.authorRamalingam,en_US
dc.contributor.authorSaraswathy, Nen_US
dc.contributor.authorSadasivam, Sen_US
dc.contributor.authorSubha, Ken_US
dc.contributor.authorPoorani, Nen_US
dc.date.accessioned2007-04-01en_US
dc.date.accessioned2009-05-27T09:30:08Z
dc.date.available2007-04-01en_US
dc.date.available2009-05-27T09:30:08Z
dc.date.issued2007-04-01en_US
dc.description.abstractalpha-Galactosidase was strongly induced in the white-rot fungus Pleurotus florida by arabinose than its natural substrates and was purified to homogeneity by acetone precipitation, ultrafiltration and DEAE-Sepharose chromatography. The enzyme was a monomeric protein with a molecular mass of approximately equal to 99 kDa, as revealed by native-PAGE and SDS-PAGE. alpha-Galactosidase was optimally active at 55 degrees C for the hydrolysis of p-nitrophenyl-alpha-galactopyranoside (PNPalphaG) and lost its 20% and 50% of original activity in 30 min at 60 degres C and 70 degrees C, respectively. The pH optimum of the enzyme was between 4.6 and 5.0. It was stable in a wide pH range (pH 4.0 to 9.0) at 55 degrees C for 2 h. The Ag+ and Hg2+ strongly inhibited the enzyme activity. Galactose, glucose, maltose and lactose also inhibited the enzyme activity, whereas N-bromosuccinimide treatment resulted in near total loss of acitivity. The Km and Vmax values of the enzyme for PNPalphaG were found to be 1.1 mM, and 77 micromol min(-1) mg(-1), respectively. alpha-Galactosidase immobilized in agar was more effective for the degradation of raffinose than in the sodium alginate. TLC results indicated its potential for the removal of raffinose and stachyose in soymilk.en_US
dc.description.affiliationDepartment of Biotechnology, Kumaraguru College of Technology, Coimbatore 641 006, Tamil Nadu, India. gobiram@rediffmail.comen_US
dc.identifier.citationRamalingam , Saraswathy N, Sadasivam S, Subha K, Poorani N. Purification and properties of alpha-galactosidase from white-rot fungus Pleurotus florida. Indian Journal of Biochemistry & Biophysics. 2007 Apr; 44(2): 76-81en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/27698
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshEnzyme Inductionen_US
dc.subject.meshEnzymes, Immobilizeden_US
dc.subject.meshFungal Proteins --biosynthesisen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshNitrophenylgalactosides --chemistryen_US
dc.subject.meshPleurotus --enzymologyen_US
dc.subject.meshPolysaccharides --metabolismen_US
dc.subject.meshSubstrate Specificityen_US
dc.subject.meshTemperatureen_US
dc.subject.meshalpha-Galactosidase --biosynthesisen_US
dc.titlePurification and properties of alpha-galactosidase from white-rot fungus Pleurotus florida.en_US
dc.typeJournal Articleen_US
Files
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.79 KB
Format:
Plain Text
Description:
Download
Collections
Indian Journal of Biochemistry & Biophysics