Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Kun Meng"'
Autor:
Bo Xu, Tu Tao, Yingguo Bai, Bin Yao, Zhiyun Wang, Kun Meng, Wang Yuan, Huiying Luo, Mengting Liu
Publikováno v:
Journal of Bioscience and Bioengineering. 129:16-22
The economical production of pectin oligosaccharides with a specific degree of polymerization and structure from agro-food waste is an industrially important process. This study identified a novel pectate lyase gene (plhy1) from the thermophilic cell
Publikováno v:
Microbial Cell Factories, Vol 18, Iss 1, Pp 1-12 (2019)
Microbial Cell Factories
Microbial Cell Factories
Background The development of sustainable technologies for plant cell wall degradation greatly depends on enzymes with hydrolytic activities against carbohydrates. The waste by-products of agricultural cereals are important biomass sources because th
Publikováno v:
Food Chemistry. 188:569-575
Polygalacturonase is one of the most important industrial pectinases. To enrich the genetic resources and develop new enzyme candidates, three polygalacturonase genes (Nfpg I–III) of glycosyl hydrolase family 28 were cloned from Neosartorya fischer
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 118:70-78
In addition to cellulose and hemicellulose, pectin is an important renewable resource for biorefinery. Endo- and exo-polygalacturonases are two essential enzymes required for complete deconstruction of pectin into simple and fermentable sugars. In bi
Publikováno v:
Food Chemistry. 162:229-234
A pectin methylesterase gene (pe8F46) was cloned from Penicillium chrysogenum F46 and successfully expressed in Pichia pastoris. The full-length cDNA consists of 969 bp and encodes a 322-residue polypeptide with the calculated molecular weight of 34.
Autor:
Yingguo Bai, Caihong Wang, Kun Meng, Huifang Hua, Kun Wang, Bin Yao, Huoqing Huang, Pengjun Shi, Huiying Luo, Niu Canfang
Publikováno v:
Applied Microbiology and Biotechnology. 99:1217-1228
Thermophilic β-mannanases are of increasing importance for wide industrial applications. In the current study, gene cloning, functional expression in Pichia pastoris, and characterization of a thermophilic β-mannanase (Man5A) from thermophilic Tala
Autor:
Rui Ma, Huiying Luo, Yingguo Bai, Pengjun Shi, Kun Meng, Yaru Wang, Peilong Yang, Tu Tao, Bin Yao
Publikováno v:
Applied Microbiology and Biotechnology. 98:5019-5028
A multimodular pectinase of glycoside hydrolase family 28, S6A, was identified in Penicillium oxalicum SX6 that consists of an N-terminal catalytic domain of pectin methylesterase, a Thr/Ser-rich linker region, and a C-terminal catalytic domain of po
Autor:
Kun Meng, Yaru Wang, Yingguo Bai, Bin Yao, Pengjun Shi, Peilong Yang, Liang Zhao, Huiying Luo, Huoqing Huang
Publikováno v:
Process Biochemistry. 48:1879-1885
Thermophilic xylanases are of great interest for their wide industrial application prospects. Here we identified a thermophilic xylanase (XynC01) of glycoside hydrolase (GH) family 10 in a thermophilic fungal strain Achaetomium sp. Xz-8. The deduced
Autor:
Kun Meng, Bin Yao, Huiying Luo, Pengjun Shi, Peilong Yang, Yaru Wang, Tu Tao, Wei Zhang, Yingguo Bai, Yuhong Zhang
Publikováno v:
Food Chemistry. 141:2974-2981
A novel endo-polygalacturonase (endo-PG I) from Achaetomium sp. Xz8 was identified, overexpressed in Pichia pastoris, and characterized in this report. Recombinant endo-PG I is distinguished from other enzyme counterparts by its high activity towards
Publikováno v:
Applied Microbiology and Biotechnology. 98:2155-2163
The gene man5XZ3 from Aspergillus nidulans XZ3 encodes a multimodular β-mannanase of glycoside hydrolase family 5 that consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain. Recombinant Man5X