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- Title
Fusion of Carbohydrate Binding Modules to Bifunctional Cellulase to Enhance Binding Affinity and Cellulolytic Activity.
- Authors
Maharjan, Anoth; Alkotaini, Bassam; Kim, Beom Soo
- Abstract
Bifunctional cellulase (glycoside hydrolase 5, GH5) from <italic>Bacillus</italic> sp. D04 having both endo- and exoglucanase activities was fused with two types of carbohydrate binding modules (CBMs). CBM3 from Bacillus sp. D04 and CBM9 from <italic>Thermotoga maritima</italic> Xyn10A were added to GH5 to hydrolyze microcrystalline cellulose (Avicel) as well as water-soluble cellulose (carboxymethyl cellulose, CMC). The optimum temperature of GH5 was 50oC, while it increased to 60oC for the fusion GH5-CBM3 and GH5-CBM9, indicating that addition of CBM increased the thermostability of the enzyme. Addition of CBM3 and CBM9 enhanced the GH5 affinity (<italic>K</italic>M), for which <italic>K</italic>M decreased from 104 to 33.9 ~ 35.1 mg/mL for CMC, and from 115 to 55.5 ~ 80.3 mg/mL for Avicel, respectively. The catalytic efficiency (<italic>k</italic>cat/<italic>K</italic>M) also increased from 4.80 to 5.36 ~ 6.46 (mL/mg)/sec for CMC, and from 1.77 to 2.40 ~ 4.45 (mL/mg)/sec for Avicel, respectively, by addition of CBM3 and CBM9.
- Publication
Biotechnology & Bioprocess Engineering, 2018, Vol 23, Issue 1, p79
- ISSN
1226-8372
- Publication type
Academic Journal
- DOI
10.1007/s12257-018-0011-4