title: Purification and characterization of a novel cellobiohydrolase (PdCel6A) from Penicillium decumbens JU-A10 for bioethanol production.
abstract: An acidic Cel6A, cellobiohydrolase (CBH) II, was purified from Penicillium decumbens and designated as PdCel6A. The deduced internal amino acid sequence of the novel CBH has a high degree of sequence identity with the CBH II from Aspergillus fumigatus. Surprisingly, PdCel6A exhibits characteristics comparable to that of CBH I, as well as CBH II. Similar to CBH I, the novel CBH has a specific activity of 1.9 IU/mg against p-nitrophenyl-β-d-cellobioside. The enzyme retains about 80% of its maximum activity after 4h of incubation at pH 2.0. Using delignified corncob residue as the substrate, ethanol concentration increased by 20% during simultaneous saccharification and fermentation when supplemented with low doses of PdCel6A (0.2mg/g substrate). To our knowledge, this is the first report involving a CBH I-like CBH II. The present paper provides new insight into the role of CBH II in cellulose degradation.
authors: State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, PR China.
authors: Le
authors: L
authors: Gao
authors: Fenghui
authors: F
authors: Wang
authors: Feng
authors: F
authors: Gao
authors: Lushan
authors: L
authors: Wang
authors: Jian
authors: J
authors: Zhao
authors: Yinbo
authors: Y
authors: Qu
mesh_terms: D000595:Amino Acid Sequence; D043366:Cellulose 1,4-beta-Cellobiosidase / Q000737:chemistry / Q000302:isolation & purification*; D000431:Ethanol / Q000378:metabolism*; D008969:Molecular Sequence Data; D010407:Penicillium / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000431:Ethanol; D043366:Cellulose 1,4-beta-Cellobiosidase