Polysaccharide hydrolases from leaves of Boscia senegalensis: properties of endo-(1-->3)-beta-D-glucanase

M.H. Dicko, M.J. Searle-van Leeuwen, A.S. Traore, M.H. Hilhorst, G. Beldman

Research output: Contribution to journalArticleAcademicpeer-review

12 Citations (Scopus)

Abstract

The leaves of Boscia senegalensis are traditionally used in West Africa in cereal protection against pathogens, pharmacologic applications, and food processing. Activities of α-amylase, β-amylase, exo-(1-->3, 1-->4)-β-D-glucanase, and endo-(1-->3)-β-D-glucanase were detected in these leaves. The endo-(1-->3)-β-D-glucanase (EC 3.2.1.39) was purified 203-fold with 57"ield. The purified enzyme is a nonglycosylated monomeric protein with a molecular mass of 36 kDa and pI ≥ 10.3. Its optimal activity occurred at pH 4.5 and 50°C. Kinetic analysis gave Vmax, kcat, and Km 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)-β-glucan chains in an endo fashion. This property is unusual for endo-acting (1-->3)-β-D-glucanase from plants. The involvement of the enzyme in plant defense against pathogenic microorganisms such as fungi is discussed.
Original languageEnglish
Pages (from-to)225-241
JournalApplied Biochemistry and Biotechnology
Volume94
Issue number3
DOIs
Publication statusPublished - 2001

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