dc.contributor.author |
AGNANTIARI, G |
en |
dc.contributor.author |
CHRISTAKOPOULOS, P |
en |
dc.contributor.author |
KEKOS, D |
en |
dc.contributor.author |
MACRIS, BJ |
en |
dc.date.accessioned |
2014-03-01T01:40:51Z |
|
dc.date.available |
2014-03-01T01:40:51Z |
|
dc.date.issued |
1991 |
en |
dc.identifier.issn |
0138-4988 |
en |
dc.identifier.uri |
https://dspace.lib.ntua.gr/xmlui/handle/123456789/23278 |
|
dc.subject.classification |
Biotechnology & Applied Microbiology |
en |
dc.subject.other |
PURIFICATION |
en |
dc.title |
A PURIFIED ALPHA-GALACTOSIDASE FROM ASPERGILLUS-NIGER WITH ENHANCED KINETIC CHARACTERISTICS |
en |
heal.type |
journalArticle |
en |
heal.language |
English |
en |
heal.publicationDate |
1991 |
en |
heal.abstract |
Extracellular alpha-galactosidase from Aspergillus niger was purified 128-fold over the crude extract by gel filtration, ion exchange chromatography and chromatofocusing. Certain substrates and end products affected enzyme activity. Among the former p-nitrophenyl-alpha-galactopyranoside (PNPG) inhibited the enzyme at 1.4 mM while melibiose did not inhibit alpha-galactosidase at concentrations up to 50 mM. Enzymic end products such as glucose did not inhibit the enzyme at concentrations up to 100 mM while galactose exhibited a competitive inhibition with a K(i) = 1.29 mM. The kinetic characteristics of the enzyme compared favourably to other microbial alpha-galactosidases and make it suitable for food process applications. |
en |
heal.publisher |
AKADEMIE VERLAG GMBH |
en |
heal.journalName |
ACTA BIOTECHNOLOGICA |
en |
dc.identifier.isi |
ISI:A1991HF98200008 |
en |
dc.identifier.volume |
11 |
en |
dc.identifier.issue |
5 |
en |
dc.identifier.spage |
479 |
en |
dc.identifier.epage |
484 |
en |