Suppression of growth defects of α-amylase secretingEscherichia coliby signal sequence fusion [PDF]
Two fusions of the Bacillus stearothermophilus α-amylase gene (amyS) with lacpoZ′ were constructed. The first, being a transcriptional fusion, placed amyS directly under lac promoter control eliminating interference by the endogenous promoter. IPTG induction of amyS transcription in this construction resulted in liberation of periplasmic proteins and ...
Ilari Suominen +4 more
openaire +1 more source
Research progress on enhancement of bacterial α-amylase activity
α-amylase is an endonuclease that acts on the α-1,4-glucoside bond of starch molecules to reduce starch viscosity. As a commonly used additive in animal feed, α-amylase can make up for the deficiency of animal amylase, accelerate the starch ...
BAI Jing, WANG Jun, LI Mo, SONG Li-li
doaj
Molecular, Biochemical, and Dietary Regulation Features of α-Amylase in a Carnivorous Crustacean, the Spiny Lobster Panulirus argus. [PDF]
Alpha-amylases are ubiquitously distributed throughout microbials, plants and animals. It is widely accepted that omnivorous crustaceans have higher α-amylase activity and number of isoforms than carnivorous, but contradictory results have been obtained ...
Leandro Rodríguez-Viera +8 more
doaj +1 more source
Effects of chickpea protein fractions on α-amylase activity in digestion
This study concerns the effects of endogenous proteins on starch digestion kinetics. It investigates the effects in chickpeas of hydrolysates released from the endogenous proteins albumin, globulin and glutelin on the in vitro activity of porcine ...
Tan, X +8 more
core +1 more source
Novel α-amylase inhibitor hemi-pyocyanin produced by microbial conversion of chitinous discards
α-Amylase inhibitors (aAIs) have been applied for the efficient management of type 2 diabetes. The aim of this study was to search for potential aAIs produced by microbial fermentation.
Nguyen TH; Wang SL; Nguyen AD; Doan MD; Tran TN; Doan CT; Nguyen VB
core +1 more source
Isolation and characterization of α ‐amylase encoding gene in Bacillus amyloliquefaciens PAS
Amylolytic bacteria are a source of amylase, which is an essential enzyme to support microalgae growth in the bioreactor for microalgae culture. In a previous study, the highest bacterial isolate to hydrolyze amylum (namely PAS) was successfully isolated
Achmad Rodiansyah +4 more
doaj +1 more source
Aspergillus favus (A. flavus) is a saprophytic fungus and a pathogen affecting several important foods and crops, including maize. A. flavus produces a toxic secondary metabolite called aflatoxin.
Chandran Remya (15544994) +3 more
core +1 more source
Cloning and expression of aBacillus licheniformisα-amylase gene inPseudomonas aeruginosa [PDF]
Abstract The gene for B. licheniformis α-amylase has been cloned in P. aeruginosa . Synthesis of the enzyme occurs in late log phase and goes on during stationary phase. Although P. aeruginosa is a secretory bacterium, α-amylase is not efficiently secreted into the extracellular medium; 85% of the enzyme is retained in the periplasm.
A. Filloux +3 more
openaire +1 more source
Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization
α-Amylase from Trichoderma harzianum was covalently immobilized on activated wool by cyanuric chloride. Immobilized α-amylase exhibited 75% of its initial activity after 10 runs.
Saleh A. Mohamed +3 more
doaj +1 more source
Postprandial hyperglycemia has orchestrated untimely death among diabetic patients over the decades and regulation of α-amylase activity is now becoming a promising management option for type 2 diabetes.
Oghenetega J. Avwioroko +8 more
doaj +1 more source

