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Titolo:
Polysaccharide hydrolases from leaves of Boscia senegalensis
Autore:
Dicko, MH; Searle-van Leeuwen, MJF; Traore, AS; Hilhorst, R; Beldman, G;
Indirizzi:
Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Labs Biochem & Food Chem, NL-6700 EV Wageningen, Netherlands Univ Wageningen & Res Ctr Wageningen Netherlands NL-6700 EV Netherlands Univ Ouagadougou, UFR SVT, Biochim Lab, Ouagadougou 03, Burkina Faso Univ Ouagadougou Ouagadougou Burkina Faso 03 uagadougou 03, Burkina Faso
Titolo Testata:
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
fascicolo: 3, volume: 94, anno: 2001,
pagine: 225 - 241
SICI:
0273-2289(200106)94:3<225:PHFLOB>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
PATHOGENESIS-RELATED PROTEINS; GERMINATED BARLEY; CELL-WALLS; PURIFICATION; BETA-1,3-GLUCANASE; ENDO-1,3-BETA-GLUCANASE; 1,3-BETA-GLUCANASES; ENDOHYDROLASE; DEGRADATION; RESISTANCE;
Keywords:
alpha-Amylase; beta-amylase; beta-glucanase; disodium 2,2 '-bichinconitate; yeast glucan; high-performance liquid chromatography; matrix-assisted laser desorption/ionization time-of-flight mass spectrometry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Beldman, G Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Labs Biochem & Food Chem, POB 8129, NL-6700 EV Wageningen, Netherlands Univ Wageningen & Res Ctr POB 8129 Wageningen Netherlands NL-6700 EV
Citazione:
M.H. Dicko et al., "Polysaccharide hydrolases from leaves of Boscia senegalensis", APPL BIOC B, 94(3), 2001, pp. 225-241

Abstract

The leaves of Boscia senegalensis are traditionally used in West Africa incereal protection against pathogens, pharmacologic applications, and food processing. Activities of alpha -amylase, beta -amylase, exo-(1 -->3, 1 -->4)-beta -D-glucanase, and endo-(1 -->3)-beta -D-glucanase were detected in these leaves. The endo-(1 -->3)-beta -D-glucanase (EC 3.2.1.39) was purified 203-fold with 57% yield. The purified enzyme is a nonglycosylated monomeric protein with a molecular mass of 36 kDa and pI greater than or equal to 10.3. Its optimal activity occurred at pH 4.5 and 50 degreesC. Kinetic analysis gave V-max, k(cat), and K-m values of 659 U/mg, 395 s(-1), and 0.42 mg/mL, respectively, for laminarin as substrate. The use of matrix-assisted laser desorption ionization time-of-flight mass spectrometry and high-performance liquid chromatography revealed that the enzyme hydrolyzes not only soluble but also insoluble (1 -->3)-beta -glucan chains in an endo fashion. This property is unusual for endo-acting (1 -->3)-beta -D-glucanase from plants. The involvement of the enzyme in plant defense against pathogenic microorganisms such as fungi is discussed.

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Documento generato il 03/04/20 alle ore 10:10:09