Production of high activity Aspergillus niger BCC4525 β-mannanase in Pichia pastoris and its application for mannooligosaccharides production from biomass hydrolysis
| العنوان: | Production of high activity Aspergillus niger BCC4525 β-mannanase in Pichia pastoris and its application for mannooligosaccharides production from biomass hydrolysis |
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| المؤلفون: | Sutipa Tanapongpipat, Piyanun Harnpicharnchai, Kittapong Sae-Tang, Wanwisa Teanngam, Warasirin Sornlake, Pennapa Manitchotpisit, Waraporn Pinngoen |
| المصدر: | Bioscience, Biotechnology, and Biochemistry. 80:2298-2305 |
| بيانات النشر: | Informa UK Limited, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 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 |
| الوصف: | 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. |
| تدمد: | 1347-6947 0916-8451 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99c0a7a3a7af23885dbe2908b12b3e43 https://doi.org/10.1080/09168451.2016.1230003 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....99c0a7a3a7af23885dbe2908b12b3e43 |
| قاعدة البيانات: | OpenAIRE |
PDF full text from Publisher | تدمد: | 13476947 09168451 |
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