Abstract
A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a monomeric enzyme with a molecular mass of 40 kDa. The optimum temperature and pH for endoglucanase activity of Cen219 was separately 50°C and 6.0. It was stable from 30 to 50°C, and from pH 4.0 to 7.0. The activity was significantly enhanced by Mn2+ and dramatically reduced by detergent SDS and metals Fe3+, Cu2+ or Hg2+. The enzyme hydrolyzed a wide range of β-1, 3-, and β-1, 4-linked polysaccharides, with varying activities. Activities towards microcrystalline cellulose and filter paper were relatively high, while the highest activity was towards oat gum. The Km and Vmax of Cen219 towards CMC was 17.37 mg/ml and 333.33 U/mg, respectively. The findings have an insight into understanding the molecular basis of host–parasite interactions in B. xylophilus species. The properties also make Cen219 an interesting enzyme for biotechnological application.
Highlights
Limited fossil resources, growing economies and an everlasting burden on our environment have caused an increasing interest for alternative resources to produce fuels and chemicals [1]
Construction and Screening of the Metagenomic Library A metagenomic library containing about 5,000 clones was constructed from Bursaphelenchus xylophilus (Bx) and its associated microbe samples
It is wellknown that Bx is an important invasive plant parasitic nematode
Summary
Limited fossil resources, growing economies and an everlasting burden on our environment have caused an increasing interest for alternative resources to produce fuels and chemicals [1]. Lignocellulose, composed mainly of cellulose, hemicellulose, and lignin, is the most abundant renewable carbon source on earth and an attractive resource to use it for the production of different chemical building blocks or biofuels [2]. Due to the compact microfibrils formation and complex crystalline organization together with the heterogeneous polysaccharide network, lignocellulosic biomass is recalcitrant to deconstruction and poorly susceptible to both chemical and enzymatic hydrolysis. Enzyme production costs and complex pretreating lignocellulosic materials with chemicals and/or heat still constitute limiting factors to wide-scale and rapid biomass conversion [6,13,14]. Searching novel cellulases from extreme and special environments becomes an attractive alternative
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