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Titolo:
Inhibition of Trichoderma cellulase activity by a stilbene glucoside from Picea glehnii bark
Autore:
Shibutani, S; Igarashi, K; Samejima, M; Saburi, Y;
Indirizzi:
Univ Tokyo, Grad Sch Agr & Life Sci, Dept Biomat Sci, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 omat Sci, Bunkyo Ku, Tokyo 1138657, Japan
Titolo Testata:
JOURNAL OF WOOD SCIENCE
fascicolo: 2, volume: 47, anno: 2001,
pagine: 135 - 140
SICI:
1435-0211(2001)47:2<135:IOTCAB>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHANEROCHAETE-CHRYSOSPORIUM; CELLOBIOSE DEHYDROGENASE; CELLOBIOHYDROLASE-I; LIMITED PROTEOLYSIS; REESEI; CRYSTALLINE; RESISTANCE; CELLULOSES; TANNINS; OXIDASE;
Keywords:
stilbene glucoside; Picea glehnii; cellulase; inhibitor; Trichoderma;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Engineering, Computing & Technology
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Samejima, M Univ Tokyo, Grad Sch Agr & Life Sci, Dept Biomat Sci, Bunkyo Ku, Tokyo 1138657, Japan Univ Tokyo Tokyo Japan 1138657 nkyo Ku, Tokyo 1138657, Japan
Citazione:
S. Shibutani et al., "Inhibition of Trichoderma cellulase activity by a stilbene glucoside from Picea glehnii bark", J WOOD SCI, 47(2), 2001, pp. 135-140

Abstract

The stilbene glucoside isorhapontin (5,4 ' -dihydroxy-3 ' -methoxystilbene-3-beta -D-glucoside) is the major constituent of the ethyl acetate extracts from Picea glehnii bark. Isorhapontin inhibited the hydrolytic activity of Trichoderma cellobiohydrolase I (CBH I) for both bacterial microcrystalline cellulose and the soluble cellooligosaccharide celloheptaitol. The inhibitory effect for celloheptaitol, however, was more drastic than that for bacterial microcrystalline cellulose. The hydrolytic activity of the CBH I core domain for celloheptaitol was also inhibited by isorhapontin to a similar extent, suggesting that the interaction between isorhapontin and the coredomain of CBH I is the reason for this phenomenon. The inhibition of CBH Iactivity by isorhapontin showed mixed noncompetitive and uncompetitive types in a concentration of the inhibitor of less than 125 muM. The K-i and K-i' values were estimated to be 57.2 and 33.3 muM, respectively. Whereas isorhapontin strongly inhibited CBH I activity, its aglycone isorhapontigenin (3 ' -methoxy-3,5,4 ' -trihydroxystilbene) showed almost no inhibition. Consequently, both the stilbenic and the beta -glucosidic structures in isorhapontin are essential for the inhibitory effect on CBH I activity. Isorhapontin also inhibited the activity of Trichoderma endoglucanase I for celloheptaitol, whereas almost no effect was observed for the activities of both endoglucanases II and III.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 01:53:53