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Titolo:
PROPERTIES OF CATHEPSIN-B IMMOBILIZED IN CALCIUM ALGINATE BEADS
Autore:
KAMBOJ RC; RAGHAV N; NANDAL A; SINGH H;
Indirizzi:
KURUKSHETRA UNIV,DEPT CHEM,BIOCHEM LAB KURUKSHETRA 132119 HARYANA INDIA
Titolo Testata:
Journal of chemical technology and biotechnology
fascicolo: 2, volume: 65, anno: 1996,
pagine: 149 - 155
SICI:
0268-2575(1996)65:2<149:POCIIC>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
PURIFICATION; MACROPHAGES; CELLS;
Keywords:
LYSOSOMAL CYSTEINE PROTEINASE; CATHEPSIN B; IMMOBILIZATION; ALGINATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
17
Recensione:
Indirizzi per estratti:
Citazione:
R.C. Kamboj et al., "PROPERTIES OF CATHEPSIN-B IMMOBILIZED IN CALCIUM ALGINATE BEADS", Journal of chemical technology and biotechnology, 65(2), 1996, pp. 149-155

Abstract

Cathepsin B (EC 3.4.22.1), purified from goat brain, was immobilized in calcium alginate beads in the presence of bovine serum albumin. Theimmobilized enzyme retained similar to 63% of the original activity and could be used for seven successive batch reactions with retention of 22-30% of the initial activity. Immobilized cathepsin B hydrolysed alpha-N-benzoyl-D,L-arginine-beta-naphthylamide (BANA) maximally at pH 5.5, exhibiting a shift of 0.5 pH unit from that of the soluble enzyme(pH optima 6.0). It showed enhanced stability in acidic as well as alkaline environments in comparison to the free enzyme. The optimal temperature and thermal stability were not altered significantly after immobilization. The K-m value for the immobilized enzyme was two-fold higher than for the soluble enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 06:54:55