Abstract：
:The Cel-BL11 gene from Paenibacillus campinasensis BL11 was cloned and expressed in Escherichia coli as a His-tag fusion protein. Zymographic analysis of the recombinant protein revealed cellulase activity corresponding to a protein with a 38-kDa molecular weight. The optimum temperature and pH for purified cellulase were 60 °C and pH 7.0, respectively. The enzyme retained more than 80% activity after 8h at 60 °C at pH 6 and 7. The cellulase has a Km of 11.25 mg/ml and a Vmax of 1250 μmol/min/mg with carboxylmethyl cellulose (CMC). Then enzyme was active on Avicel, swollen Avicel, CMC, barley β-glucan, laminarin in the presence of 100 mM acetate buffer. It was inhibited by Hg²⁺, Cu²⁺ and Zn²⁺. Significant kraft pulp refining energy saving, 10%, was exhibited by the pretreatment of this cellulase applied at 2 IU per gram of oven-dried pulp. Broad pH and temperature stability render this cellulase a convenient applicability toward current mainstream biomass conversion and other industrial processes.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Ko CH,Tsai CH,Lin PH,Chang KC,Tu J,Wang YN,Yang CYdoi
10.1016/j.biortech.2010.05.043subject
Has Abstractpub_date
2010-10-01 00:00:00pages
7882-8issue
20eissn
0960-8524issn
1873-2976pii
S0960-8524(10)00899-0journal_volume
101pub_type
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