Results 21 to 30 of about 48,930 (267)

Cloning and expression of aBacillus licheniformisα-amylase gene inPseudomonas aeruginosa [PDF]

FEMS Microbiology Letters, 1985
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, P. Joyet, M. Murgier, A. Lazdunski   +3 more
openaire   +1 more source

Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization

Molecules, 2014
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, Jalaluddin A. Khan, Omar A. M. Al-Bar, Reda M. El-Shishtawy   +3 more
doaj   +1 more source

Exploring the binding interactions of structurally diverse dichalcogenoimidodiphosphinate ligands with α-amylase: Spectroscopic approach coupled with molecular docking

Biochemistry and Biophysics Reports, 2020
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, Temidayo T. Oyetunde, Francis O. Atanu, Chiagoziem A. Otuechere, Akpovwehwee A. Anigboro, Oluropo F. Dairo, Akpoyovware S. Ejoh, Sunday O. Ajibade, Martins O. Omorogie   +8 more
doaj   +1 more source

Transfer of the effect of potentized Mercuric chloride on α-amylase from one test tube to another through capillary water.

International Journal of High Dilution Research - ISSN 1982-6206, 2021
Objective: In a series of experiments we showed that treatment of a plant or animal with a diluted and agitated substance might affect other plants or animals connected to the former by the capillary water in cotton threads. The aim of the present study was to establish whether drug effect could be transferred in a cell-free medium. Design:
Atheni Konar, Tandra Sarkar, Nirmal Chandra Sukul, Anirban Sukul, Indrani Chakraborty   +4 more
openaire   +2 more sources

Enhanced extracellular expression of Bacillus stearothermophilus α-amylase in Bacillus subtilis through signal peptide optimization, chaperone overexpression and α-amylase mutant selection

Microbial Cell Factories, 2019
Background Our laboratory has constructed a Bacillus stearothermophilus α-amylase (AmyS) derivative with excellent enzymatic properties. Bacillus subtilis is generally regarded as safe and has excellent protein secretory capability, but heterologous ...
Dongbang Yao, Lingqia Su, Na Li, Jing Wu
doaj   +1 more source

Synthesis and Molecular Docking Studies of Alkoxy- and Imidazole-Substituted Xanthones as α-Amylase and α-Glucosidase Inhibitors

Molecules, 2023
Current antidiabetic drugs have severe side effects, which may be minimized by new selective molecules that strongly inhibit α-glucosidase and weakly inhibit α-amylase.
Dolores G. Aguila-Muñoz, Gabriel Vázquez-Lira, Erika Sarmiento-Tlale, María C. Cruz-López, Fabiola E. Jiménez-Montejo, Víctor E. López y López, Carlos H. Escalante, Dulce Andrade-Pavón, Omar Gómez-García, Joaquín Tamariz, Aarón Mendieta-Moctezuma   +10 more
doaj   +1 more source

Nucleotide sequence of the extracellular α-amylase gene in the yeastSchwanniomyces occidentalisATCC 26077 [PDF]

FEMS Microbiology Letters, 1992
The Schwanniomyces occidentalis (formerly castellii) ATCC 26077 (CBS 2863) alpha-amylase (AMY 26077) gene was cloned in Saccharomyces cerevisiae and sequenced. An open-reading frame encoding the AMY consists of 1536 base pairs and contains 512 amino-acid residues, which is almost the same in size as the AMY of Sch.
null Jong Chun Park, null Suk Bai, null Chi Youn Tai, null Soon Bai Chun   +3 more
openaire   +1 more source

BIOCHEMICAL STUDIES ON α-AMYLASE INHIBITOR EXTRACTED FROM WHITE KIDNEY BEAN (Phaseolus vulgaris) [PDF]

Journal of Agricultural Chemistry and Biotechnology, 2014
  Crude extract of white kidney beans (Phaseolus vulgaris) showed inhibitory activity against porcine pancreatic α-amylase and human salivary α-amylase.
Nancy A.A. Taha, A.M. Yussef, N.S. Eryan, L.K. Tadros   +3 more
doaj   +1 more source

Concurrent occurrence of α-amylase inhibitor and stimulator in red kidney bean seed: physiological implications

Biologia Plantarum, 2010
It is hypothesized that since protein α-amylase inhibitor (α-AI) and stimulator might be present together in red kidney bean (Phaseolus vulgaris L.) seeds, their in vitro interactions might influence their detection and quantification.
H. Alizadeh, D. W. M. Leung, A. L. J. Cole   +2 more
doaj   +1 more source

Heterologous expression, biochemical characterization, and overproduction of alkaline α-amylase from Bacillus alcalophilus in Bacillus subtilis

Microbial Cell Factories, 2011
Background Alkaline α-amylases have potential applications for hydrolyzing starch under high pH conditions in the starch and textile industries and as ingredients in detergents for automatic dishwashers and laundries.
Li Jianghua, Liu Long, Yang Haiquan, Du Guocheng, Chen Jian   +4 more
doaj   +1 more source