EXCEPTIONALLY THERMOSTABLE ALPHA-GALACTOSIDASE AND BETA-GALACTOSIDASE FROM ASPERGILLUS-NIGER SEPARATED IN ONE-STEP

CHRISTAKOPOULOS, P; MACRIS, BJ; KEKOS, D

dc.contributor.author	CHRISTAKOPOULOS, P	en
dc.contributor.author	MACRIS, BJ	en
dc.contributor.author	KEKOS, D	en
dc.date.accessioned	2014-03-01T01:40:10Z
dc.date.available	2014-03-01T01:40:10Z
dc.date.issued	1990	en
dc.identifier.issn	0032-9592	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/23084
dc.subject.classification	Biochemistry & Molecular Biology	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Engineering, Chemical	en
dc.subject.other	PURIFICATION	en
dc.subject.other	LACTASE	en
dc.subject.other	WHEY	en
dc.title	EXCEPTIONALLY THERMOSTABLE ALPHA-GALACTOSIDASE AND BETA-GALACTOSIDASE FROM ASPERGILLUS-NIGER SEPARATED IN ONE-STEP	en
heal.type	journalArticle	en
heal.language	English	en
heal.publicationDate	1990	en
heal.abstract	Extracellular alpha- and-beta-galactosidases from a strain of Aspergillus niger were separated and purified in one step by cation exchange chromatography. Both enzymes had acidic pH (3.5-4.0) and high temperature (65-degrees-C) optima and an exceptionally high thermostability. Thus, -alpha-galactosidase had an activity half-time of 104 min at 60-degrees-C whereas at the same temperature the respective value for-beta-galactosidase was 835 min. At optimum conditions of activity the apparent K(m) values of alpha- and beta-galactosidase were 0.44mM and 1.1mM respectively. Both the high temperature optima and thermostability properties of the enzymes make them particularly suitable for high temperature processes.	en
heal.publisher	ELSEVIER SCI LTD	en
heal.journalName	PROCESS BIOCHEMISTRY	en
dc.identifier.isi	ISI:A1990EU36400003	en
dc.identifier.volume	25	en
dc.identifier.issue	6	en
dc.identifier.spage	210	en
dc.identifier.epage	212	en