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Identification and Manipulation of Subsite Structure and Starch Granule Binding Site in Plant α-Amylase
α-amylase subsite starch granule
2008/4/20
In germinating plant seeds, α-amylases degrade starch accumulated in seeds, and that requires two functions: catalysis itself and starch granule binding ability. All plant α-amylases belong to the α-a...
Improvement of the Thermal Stability of a Calcium-free, Alkaline α-Amylase by Site-directed Mutagenesis
Bacillus alkaliphile α-amylase thermostability site-directed mutagenesis
2008/4/20
Alkaline α-amylase from Bacillus sp. strain KSM-K38 (AmyK38) is a calcium-free enzyme that is stable against chelating and oxidative reagents. Recently, the thermostability of this enzyme was improved...
Determination and Analysis of the Starch Binding Domain of Streptococcus bovis 148 Raw-Starch-Hydrolyzing α-Amylase
Streptococcus bovis α-amylase linker starch binding domain CBM26
2008/4/20
We analyzed the functional structure of Streptococcus bovis 148 α-amylase (AmyA) to determine the starch binding domain (SBD) of this enzyme. Several derivative AmyAs and putative SBD segments were co...
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...
Amylase Activities and Values in Hot and Cold Water Extracts of Pearl Millet
amylase pearl millet malting water extracts
2008/4/20
Amylase activities from various cultivars of pearl millet and a sorghum cultivar and their values in cold water and hot water extracts were studied. The α-amylase and β-amylase activities and values i...
An Oxidation Stable and Chelator-resistant, Calcium-free α-Amylase from the Alkaliphilic Bacillus Isolate KSM-K38
calcium-free α-amylase Bacillus oxidative stability chelator resistance
2008/4/20
We found a novel α-amylase (AmyK38) in a culture of a novel, alkaliphilic Bacillus sp. strain KSM-K38. The enzyme was an alkaline, liquefying α-amylase, having a pH optimum of 8.0-9.5, and exhibiting ...
Engineering Thermus Maltogenic Amylase with Improved Thermostability: Probing the Role of the Conserved Calcium Binding Site in Cyclodextrin-degrading Enzymes
calcium binding site cyclodextrin-degrading enzymes mutagenesis thermostability Thermus maltogenic amylase
2008/4/20
Thermus maltogenic amylase (ThMA), one of the cyclodextrin (CD)-degrading enzymes, is expected to have a calcium-binding site (Ca2 site) based on multiple sequence alignments. In spite of the presumpt...
Measurement of the Concentration of Bioactive Gibberellin in Germinating Rice Seed Using the α-Amylase Induction from Aleurone Cells
rice, aleurone cells α-amylase bioactive GA
2008/4/20
Measurement of the concentrations of bioactive gibberellin (GA) in germinating cereal seeds is important to grasp the molecular mechanisms of storage starch degradation following the activation of ale...
Molecular Modeling and Implications of a Bacillus α-Amylase that Acquires Enhanced Thermostability and Chelator Resistance by Deletion of an Arginine-glycine Residue
α-amylase homology modeling molecular dynamics simulation thermostability chelator resistance
2008/4/20
Resistance to chelators, as well as thermostability, of an alkaline α-amylase (AmyK, formerly named LAMY) from an alkaliphilic Bacillus sp. strain was significantly improved by deletion of Arg181-Gly1...
Mutagenesis and Structural Analysis of Thermoactinomyces vulgaris R-47 α-Amylase II (TVA II)
TVA II subsite substrate recognition α-amylase family
2008/4/20
An α-amylase II (TVA II) produced by Thermoactinomyces vulgaris R-47 exhibits wide substrate specificity for starch, pullulan, cyclodextrins and isopanose. Asp465 and Arg469 are located at subsite (-2...
The Concept of the α-Amylase Family: A Rational Tool for Interconverting Glucanohydrolases/Glucanotransferases, and Their Specificities
α-amylase family neopullulanase catalytic mechanism catalytic machinery protein engineering
2008/4/19
We found a new enzyme, neopullulanase (EC 3.2.1.135), and showed that it catalyzes the hydrolysis of α-1,4- and α-1,6-glucosidic linkages, as well as transglycosylation to form α-1,4- and α-1,6-glucos...
α-Amylase Affects Starch Accumulation in Rice Grains
α-amylase Oryza sativa L. ripening seeds starch transgenic plant
2008/4/10
isoforms I-1 and II-4 were found in rice grains during ripening, α-amylase II-4 being the most predominant isoform. To determine their functions in ripening seeds, we generated a series of transgenic ...