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Bin Yao

Publications -  6
Citations -  143

Bin Yao is an academic researcher. The author has contributed to research in topics: Pichia pastoris & Enzyme. The author has an hindex of 6, co-authored 6 publications receiving 117 citations.

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Acidic β-mannanase from Penicillium pinophilum C1: Cloning, characterization and assessment of its potential for animal feed application

TL;DR: The β-mannanase gene, man5C1, was cloned from Penicillium pinophilum C1, a strain isolated from the acidic wastewater of a tin mine in Yunnan, China, and expressed in Pichia pastoris and was adaptable to a wide range of acidity, retaining >60% of its maximum activity at pH 3.0.
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Biochemical characterization of a novel thermophilic α-galactosidase from Talaromyces leycettanus JCM12802 with significant transglycosylation activity.

TL;DR: Purified recombinant Aga27A (rAga27A) was thermophilic and thermotolerant, exhibiting the maximum activity at 70°C and retaining stability at 65°C, and will be ideal for applications in various industries, especially for the synthesis of galactooligosaccharides.
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Cloning, over-expression and characterization of an alkali-tolerant endo-β-1,4-mannanase from Penicillium freii F63.

TL;DR: The recombinant enzyme, rMan5F63, was cloned from Penicillium freii F63 and overexpressed in Pichia pastoris and exhibited good stability over a broad pH range from acidic to alkaline and was cost-effective to commercialization and valuable in various industries.
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Production pectin oligosaccharides using Humicola insolens Y1-derived unusual pectate lyase.

TL;DR: High performance anion exchange chromatography-pulsed amperometric detector and ultra high performance liquid chromatography in combination with electrospray ionization tandem mass spectrometry analysis showed that galacturonic acid-oligosaccharides were the major hydrolysates produced by the degradation of apple peel pectin by PLHY1.
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Heterologous production of an acidic thermostable lipase with broad-range pH activity from thermophilic fungus Neosartorya fischeri P1.

TL;DR: The high-level expression and excellent properties of purified recombinant LIP09 make it a potential enzyme candidate in food and feed industries.