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Titolo:
PURIFICATION AND CHARACTERIZATION OF NEW TREHALOSE-PRODUCING ENZYMES ISOLATED FROM THE HYPERTHERMOPHILIC ARCHAE, SULFOLOBUS-SOLFATARICUS KM1
Autore:
KATO M; MIURA Y; KETTOKU M; SHINDO K; IWAMATSU A; KOBAYASHI K;
Indirizzi:
KIRIN BREWERY CO LTD,APPL BIORES CTR,3 MIYAHARA CHO TAKASAKI GUMMA 37012 JAPAN KIRIN BREWERY CO LTD,APPL BIORES CTR TAKASAKI GUMMA 37012 JAPAN KIRIN BREWERY CO LTD,PHARMACEUT RES LABS TAKASAKI GUMMA 37012 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,KANAZAWA KU YOKOHAMA KANAGAWA 236 JAPAN
Titolo Testata:
Bioscience, biotechnology, and biochemistry
fascicolo: 3, volume: 60, anno: 1996,
pagine: 546 - 550
SICI:
0916-8451(1996)60:3<546:PACONT>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Keywords:
TREHALOSE; SULFOLOBUS SOLFATARICUS; GLYCOSYLTREHALOSE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
9
Recensione:
Indirizzi per estratti:
Citazione:
M. Kato et al., "PURIFICATION AND CHARACTERIZATION OF NEW TREHALOSE-PRODUCING ENZYMES ISOLATED FROM THE HYPERTHERMOPHILIC ARCHAE, SULFOLOBUS-SOLFATARICUS KM1", Bioscience, biotechnology, and biochemistry, 60(3), 1996, pp. 546-550

Abstract

Amylolytic activity that converts soluble starch to alpha,alpha-trehalose (trehalose), was found in the cell homogenate of the hyperthermophilic acidophilic archae, Sulfolobus solfataricus KM1. DEAE chromatography of the homogenate as well as other new reliable assay methods showed two enzymes to be essential for this activity. These enzymes, a glycosyltransferase and an amylase, were purified to homogeneity and characterized. Their molecular masses were 76 kDa and 61 kDa and activities were maximal at 70-80 degrees C and 70-85 degrees C, respectively. High thermostability was noted for each. The reaction products by the two enzymes on maltooligosaccharides were identified by H-1- and C-13-NMR spectra and HPLC analysis. The cooperative mechanism of the two enzymes was used in a new enzymatic pathway for trehalose synthesis fromstarch.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 09:52:31