搜索结果: 1-5 共查到“制糖技术 purification”相关记录5条 . 查询时间(0.101 秒)
Purification and Characterization of Alkali-stable β-Amylase from Chinese Yam (Nagaimo) Tuber
Rare Sugar Research Center Kagawa University
2008/4/20
An alkali-stable β-amylase was purified from Nagaimo, a cultivar of yam (Dioscorea opposita Thunb.) by hexadecyltrimethylammonium bromide treatment, ammonium sulfate fractionation, and two-step column...
Purification and Characterization of an Exo-1,5-α-L-Arabinanase from Aspergillus sojae
amylopectin cluster rice starch branching enzyme starch debranching enzyme starch synthase
2008/4/20
An exo-1,5-α-L-arabinanase was purified as an electrophoretically homogenous protein from a liquid culture of Aspergillus sojae. The molecular mass of the purified enzyme was estimated to be 41 kDa by...
Purification and Characterization of Maltotriose-producing Amylases from an Alkaliphilic Nocardiopsis sp. TOA-1
maltotriose-producing amylase alkaline enzyme alkaliphilic Nocardiopsis sp.
2008/4/20
An alkaliphilic actinomycete, Nocardiopsis sp. strain TOA-1, produced extracelluar maltotriose-producing amylases. Two amylases (AmyA-1 and AmyA-2) were purified to homogeneity by three steps of chrom...
Recombinant α-Glucosidase from Aspergillus niger. Overexpression by Emericella nidulans, Purification and Characterization
α-glucosidase Aspergillus niger recombinant enzyme enzyme expression enzyme characterization
2008/4/20
An expression plasmid containing the aglA gene encoding Aspergillus niger GN-3 α-glucosidase was constructed and inserted into Emericella nidulans JCM10259. The transformant secreted about 61 mg/L of ...
Screening, Purification and Characterization of a Prokaryotic Isoprimeverose-producing Oligoxyloglucan Hydrolase from Oerskovia sp. Y1
isoprimeverose-producing oligoxyloglucan hydrolase xyloglucan isoprimeverose
2008/4/20
Isoprimeverose-producing oligoxyloglucan hydrolase (IPase; EC 3.2.1.120) is a unique β-glycosidase that cleaves xyloglucan oligosaccharides at the non-reducing end, producing isoprimeverose. Here, we ...