Purification and characterization of a cellulolytic multienzyme complex produced by Neocallimastix patriciarum J11

• Published in: Biochemical and biophysical research communications Vol. 451; no. 2; pp. 190 - 195
• Main Authors: Wang, Hui-Chang, Chen, Yo-Chia, Hseu, Ruey-Shyang
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 22.08.2014
• Subjects: Anaerobic fungi; Animals; beta-glucanase; Blotting, Western; Buffaloes - microbiology; carbon; Cellulases - genetics; Cellulases - isolation & purification; Cellulases - metabolism; cellulose; Cellulosome; Chromatography, Gel; endo-1,4-beta-glucanase; ethanol production; Fungal Proteins - genetics; Fungal Proteins - isolation & purification; Fungal Proteins - metabolism; industrial applications; lignocellulose; liquid chromatography; mass spectrometry; Multienzyme complex; Multienzyme Complexes - genetics; Multienzyme Complexes - isolation & purification; Multienzyme Complexes - metabolism; Neocallimastix; Neocallimastix - enzymology; Neocallimastix - isolation & purification; Neocallimastix patriciarum; peptides; polyacrylamide gel electrophoresis; Protein Subunits; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Renewable energy; Rumen - microbiology; rumen fungi; sodium dodecyl sulfate; sugars; Tandem Mass Spectrometry; Cellulosome; Anaerobic fungi; Multienzyme complex; Renewable energy; Neocallimastix patriciarum

•Multienzyme complexes of 670-kDa were purified from N. patriciarum J11.•Scaffolding protein exists in the multienzyme complex.•The multienzyme complex consisted of at least three types of cellulase. Understanding the roles of the components of the multienzyme complex of the anaerobial cellulase sys...