Journal
ENZYME AND MICROBIAL TECHNOLOGY
Volume 78, Issue -, Pages 1-9Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2015.06.007
Keywords
Endo-beta-1,4-mannanase; Glycoside hydrolase family 5 (GH5); Recombinant expression; Enzyme properties; Oligosaccharides preparation
Categories
Funding
- Special Fund for Agro-Scientific Research in the Public Interest [20130315]
- Fundamental Research Funds for the Central Universities [KYZ201404]
- National Natural Science Foundation of China [31100056]
- Doctoral Fund of Ministry of Education of China [20100097120011]
- National High-Tech R&D Program of China [2012AA101504]
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A novel thermostable mannanase from a newly isolated Bacillus pumilus GBSW19 has been identified, expressed, purified and characterized. The enzyme shows a structure comprising a 28 amino acid signal peptide, a glycoside hydrolase family 5 (GH5) catalytic domain and no carbohydrate-binding module. The recombinant mannanase has molecular weight of 45 kDa with an optimal pH around 6.5 and is stable in the range from pH 5-11. Meanwhile, the optimal temperature is around 65 degrees C, and it retains 50% relative activity at 60 degrees C for 12h. In addition, the purified enzyme can be activated by several ions and organic solvents and is resistant to detergents. Bpman5 can efficiently convert locus bean gum to mainly M2, M3 and M5, and hydrolyze manno-oligosaccharides with a minimum DP of 3. Further exploration of the optimum condition using HPLC to prepare oligosaccharides from locust bean gum was obtained as 10 mg/ml locust bean gum incubated with 10 U/mg enzyme at 50 degrees C for 24h. By using this enzyme, locust bean gum can be utilized to generate high value-added oligosaccharides with a DP of 2-6. (C) 2015 Elsevier Inc. All rights reserved.
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