نتایج جستجو برای: glucoamylase i

تعداد نتایج: 1039473  

Journal: :Protein expression and purification 2003
Kalyani Mondal Aparna Sharma Munishwar Nath Gupta

Starch-degrading enzymes glucoamylase (from Aspergillus niger), and pullulanase (from Bacillus acidopullulyticus) were purified using alginates (polysaccharides consisting of mannuronic acids and guluronic acids) by a recently developed technique called macroaffinity ligand-facilitated three-phase partitioning (MLFTPP). In this process, a crude preparation of the enzyme was mixed with alginate....

Journal: :Bioscience, biotechnology, and biochemistry 2005
Shota Tanimoto Hideyuki Matsumoto Kazuyoshi Fujii Ritsushi Ohdoi Koji Sakamoto Shinya Izuwa Yuichi Yamane Masaki Miyake Mitsuya Shimoda Yutaka Osajima

The Inactivation kinetics of alpha-glucosidase, glucoamylase, alpha-amylase, and acid carboxypeptidase in fresh sake using a continuous flow system for high-pressure carbonation were investigated. In addition, the effects of ethanol and sugar concentrations on inactivation of the enzymes in high-pressure carbonated sake were investigated. Among the enzymes investigated, alpha-glucosidase was th...

2012
Krystyna Żółtowska Zbigniew Lipiński Elżbieta Łopieńska-Biernat Marek Farjan Małgorzata Dmitryjuk

The activity of glycogen Phosphorylase and carbohydrate hydrolyzing enzymes α-amylase, glucoamylase, trehalase, and sucrase was studied in the development of the Carniolan honey bee, Apis mellifera carnica Pollman (Hymenoptera: Apidae), from newly hatched larva to freshly emerged imago of worker and drone. Phosphorolytic degradation of glycogen was significantly stronger than hydrolytic degrada...

Journal: :Acta crystallographica. Section F, Structural biology and crystallization communications 2011
Jaeyong Lee Mark Paetzel

Glucoamylase from Aspergillus niger is an industrially important biocatalyst that is utilized in the mass production of glucose from raw starch or soluble oligosaccharides. The G1 isoform consists of a catalytic domain and a starch-binding domain connected by a heavily glycosylated linker region. The amino-terminal catalytic domain of the G1 isoform generated by subtilisin cleavage has been cry...

Journal: :Molekuliarnaia biologiia 2007
D G Naumov

Maltase-glucoamylase and sucrase-isomaltase are two human glycosidases responsible for starch digestion. We have performed a comparative analysis of their amino acid sequences from several species of mammals and their orthologues from other chordates. This allowed us to determine the evolutionary history of the enzymes. Both glycosidases are paralogues and contain GH31 family catalytic domains....

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