標題: Catalytic function of a newly purified exo-beta-D-glucosaminidase from the entomopathogenic fungus Paecilomyces lilacinus
作者: Chao, Cheng-Fu
Chen, Yi-Yun
Cheng, Chih-Yu
Li, Yaw-Kuen
應用化學系
Department of Applied Chemistry
關鍵字: Glycohydrolase;Exo-beta-D-glucosaminidase;Transglycosylation;Mass spectrometry;GlcN-GlcNAc-butyl;Paecilomyces lilacinus
公開日期: 2-四月-2013
摘要: An entomopathogenic fungus, Paecilomyces lilacinus, was found to grow on chitosanase-detecting plates. Besides an endo-chitosanase, an exo-beta-D-glucosaminidase was purified by cation-exchange chromatography from this microorganism cultivated in M9 minimal media containing 0.5% chitosan as the sole carbon source. The molecular weight of the enzyme is 95 kDa; the optimum pH and temperature for activity are 6.0 and 45 degrees C, respectively. The purified exo-beta-D-GlcNase promotes the hydrolysis of 95% deacetylated chitosan from its non-reducing end and liberates 2-amino-2-deoxy-D-glucopyranose (GlcN) as the sole product; however, 2-acetamido-2-deoxy-D-glucopyranose (GlcNAc) was not detected when chitin was used as the substrate. The cleavage pattern confirmed using real-time mass spectrometry shows that exo-beta-D-glucosaminidase cleaves the glycosidic bonds between GlcN-GlcN and GlcN-GlcNAc but not between GlcNAc-GlcN or GlcNAc-GlcNAc. In the presence of a 10% solution of various alcohols, many alkyl-beta-D-glucosaminides were obtained, indicating that exo-beta-D-glucosaminidase is a retaining enzyme. (c) 2012 Elsevier Ltd. All rights reserved.
URI: http://dx.doi.org/10.1016/j.carbpol.2012.12.030
http://hdl.handle.net/11536/21678
ISSN: 0144-8617
DOI: 10.1016/j.carbpol.2012.12.030
期刊: CARBOHYDRATE POLYMERS
Volume: 93
Issue: 2
起始頁: 615
結束頁: 621
顯示於類別:期刊論文


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  1. 000317148200034.pdf