Enhanced thermostability of mesophilic endoglucanase Z with a high catalytic activity at active temperatures
- Authors
- Kim, Su Jung; Joo, Ji Eun; Jeon, Sang Duck; Hyeon, Jeong Eun; Kim, Seung Wook; Um, Young Soon; Han, Sung Ok
- Issue Date
- 5월-2016
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- EngZ; Thermostability; Cellulolytic efficiency; Family 9 endoglucanase; Site-directed mutagenesis
- Citation
- INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, v.86, pp.269 - 276
- Indexed
- SCIE
SCOPUS
- Journal Title
- INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
- Volume
- 86
- Start Page
- 269
- End Page
- 276
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/88706
- DOI
- 10.1016/j.ijbiomac.2016.01.068
- ISSN
- 0141-8130
- Abstract
- This is the first study for therrmostable mutants of mesophilic endoglucanase EngZ from Clostridium cellulovorans using by site-directed mutagenesis. K94R, S365P and their double mutant K94R/S365P had a wide range of active temperatures (30-60 degrees C). In addition, the optimal temperature of K94R/S365P was increased by 7.5 degrees C. K94R/S365P retained 78.3% relative activity at 70 degrees C, while the wild type retained only 5.8%. Especially, K94R/S365P remained 45.1-fold higher activity than the wild type at 70 degrees C. In addition, K94R/S365P was 3.1-fold higher activity than the wild type at 42.5 degrees C, which is the optimal temperature of the wild type. K94R/S365P showed also stimulated in 2.5-fold lower concentration of CaCl2 and delayed aggregation temperature in the presence of CaCl2 compared to the wild type. In pH stability, K94R/S365P was not influenced, but the optimum pH was transferred from pH 7 to pH 6. In long-term hydrolysis, K94R/S365P reduced the newly released reducing sugar yields after 12 h reaction; however, the yields consistently increased until 72 h. Finally, the total reducing sugar of K94R/S365P was 5.0-fold higher than the wild type at 50 degrees C, pH6. EngZ (K94R/S365P) can support information to develop thermostability of GH9 endoglucanase with a high catalytic efficiency as the potential industrial bioprocess candidate. (C) 2016 Elsevier B.V. All rights reserved.
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Collections - College of Life Sciences and Biotechnology > Division of Biotechnology > 1. Journal Articles
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