Journal
EUROPEAN FOOD RESEARCH AND TECHNOLOGY
Volume 240, Issue 4, Pages 671-677Publisher
SPRINGER
DOI: 10.1007/s00217-014-2369-7
Keywords
Bacillus subtilis WD23; Pichia pastoris GS115; Purification; Recombinant mannanase
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Funding
- state forestry administration project 948 [2012-4-03]
- National Natural Science Foundation [31170553, 30671702, 30170775]
- excellent creative talents supporting program of Heilongjiang University of Chinese Medicine [2012RCQ13]
- Fundamental Research Funds for the Central Universities [DL12CA08]
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Endo-1,4-beta-mannanases have a wide range of potential industrial applications. It was mainly used for the production of functional oligosaccharides in the food industry. In order to increase the production of endo-1,4-beta-mannanases, inducible and constitutive expression of a novel endo-1,4-beta-mannanase from Bacillus subtilis WD23 in Pichia pastoris GS115 was performed and the recombinant enzyme was characterized. The recombinant mannanase gene was successfully expressed in a fully active form in P. pastoris GS115, and the activity of recombinant mannanase reached to 5,156.742 U/mL, which was higher than those from other recombinant system. Optimal purified enzyme activity was detected at pH 6.3 and 70 A degrees C, and the purified enzyme displayed broad temperature stability (40-70 A degrees C). 150 mg/mL NaCl could still improve the activity of the enzyme. Flight mass spectrometry determination confirmed that recombinant proteins are mannanase.
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