ISSN:
0006-3592
Schlagwort(e):
recombinant β-galactosidase fusion protein
;
chelating peptide
;
immobilized metal affinity chromatography
;
immobilized enzyme
;
Chemistry
;
Biochemistry and Biotechnology
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Biologie
,
Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
Notizen:
The strong interaction of hexa-histidine fusion proteins with metal chelate adsorbents was utilized to immobilize β-galactosidase with a hexa-histidine peptide at the N-terminus to the Ni2+-nitrilotriacetic acid adsorbent. The fusion protein was cloned and expressed in Escherichia coli. The purified soluble fusion protein showed the same specific activity as the purified β-galactosidase and retained 64 percent of its β-galactosidase activity when bound to the adsorbent. To demonstrate the potential of the immobilized β-galactosidase in organic chemistry, allyl-β-D-galactosidase was synthesized from lactose and allyl alcohol on a gram scale. The same enzyme preparation was reused in three subsequent batches to prepare the model compound with high yield. © 1993 John Wiley & Sons, Inc.
Zusätzliches Material:
4 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/bit.260420205
Permalink
