Production of high activity Aspergillus niger BCC4525 β-mannanase in Pichia pastoris and its application for mannooligosaccharides production from biomass hydrolysis
| Autor: | Sutipa Tanapongpipat, Piyanun Harnpicharnchai, Kittapong Sae-Tang, Wanwisa Teanngam, Warasirin Sornlake, Pennapa Manitchotpisit, Waraporn Pinngoen |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Feed additive Oligosaccharides Applied Microbiology and Biotechnology Biochemistry Pichia Analytical Chemistry Pichia pastoris 03 medical and health sciences chemistry.chemical_compound Hydrolysis Biomass Enzyme kinetics Cloning Molecular Molecular Biology chemistry.chemical_classification biology Organic Chemistry Aspergillus niger Temperature beta-Mannosidase Substrate (chemistry) Agriculture General Medicine Hydrogen-Ion Concentration biology.organism_classification Recombinant Proteins 030104 developmental biology Enzyme chemistry Locust bean gum Mannose Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 80:2298-2305 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1080/09168451.2016.1230003 |
| Popis: | A cDNA encoding β-mannanase was cloned from Aspergillus niger BCC4525 and expressed in Pichia pastoris KM71. The secreted enzyme hydrolyzed locust bean gum substrate with very high activity (1625 U/mL) and a relatively high kcat/Km (461 mg−1 s−1 mL). The enzyme is thermophilic and thermostable with an optimal temperature of 70 °C and 40% retention of endo-β-1,4-mannanase activity after preincubation at 70 °C. In addition, the enzyme exhibited broad pH stability with an optimal pH of 5.5. The recombinant enzyme hydrolyzes low-cost biomass, including palm kernel meal (PKM) and copra meal, to produce mannooligosaccharides, which is used as prebiotics to promote the growth of beneficial microflora in animals. An in vitro digestibility test simulating the gastrointestinal tract system of broilers suggested that the recombinant β-mannanase could effectively liberate reducing sugars from PKM-containing diet. These characteristics render this enzyme suitable for utilization as a feed additive to improve animal performance. A recombinant β-mannanase from A. niger BCC4525 exhibits high activity. It produces MOS from low-cost biomass and enhance the release of reducing sugars from diet. |
| Databáze: | OpenAIRE |
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