Results 21 to 30 of about 84,224 (310)

α-Amylase inhibitors : a review of raw material and isolated compounds from plant source [PDF]

, 2012
Inhibition of α-amylase, enzyme that plays a role in digestion of starch and glycogen, is considered a strategy for the treatment of disorders in carbohydrate uptake, such as diabetes and obesity, as well as, dental caries and periodontal diseases ...
Batista, Pérola de Oliveira Magalhães Dias, Sales, Paloma Michelle de, Silveira, Dâmaris, Simeoni, Luiz Alberto, Souza, Paula Monteiro de   +4 more
core   +2 more sources

Isolation and characterization of α ‐amylase encoding gene in Bacillus amyloliquefaciens PAS

Indonesian Journal of Biotechnology, 2021
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, Sitoresmi Prabaningtyas, Mastika Marisahani Ulfah, Ainul Fitria Mahmuda, Uun Rohmawati   +4 more
doaj   +1 more source

Inhibition of Digestive Enzymes and Antioxidant Activity of Extracts from Fruits of Cornus alba, Cornus sanguinea subsp. hungarica and Cornus florida - A Comparative Study [PDF]

, 2020
The fruits of some Cornus species (dogwoods) are used in traditional medicine and considered potential anti-diabetic and hypolipemic agents. The aim of the study was to determine the ability of extracts from Cornus alba (CA), Cornus florida (CF), and ...
Buchholz, Tina, Czerwińska, Monika E., Melzig, Matthias F., Stanisławska, Iwona, Truba, Joanna, Walasek, Marta, Wieczorkowska, Wioleta, Woliński, Konrad   +7 more
core   +1 more source

Suppression of growth defects of α-amylase secretingEscherichia coliby signal sequence fusion [PDF]

FEMS Microbiology Letters, 1988
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, Jarmo Käpylä, Carola Tilgmann, Virpi Glumoff, Pekka Mäntsälä   +4 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

Glycogenin is Dispensable for Glycogen Synthesis in Human Muscle, and Glycogenin Deficiency Causes Polyglucosan Storage [PDF]

, 2020
Glycogenin is considered to be an essential primer for glycogen biosynthesis. Nevertheless, patients with glycogenin-1 deficiency due to biallelic GYG1 (NM_004130.3) mutations can store glycogen in muscle.
Dellgren, Göran, Glamuzina, Emma, Hedberg-Oldfors, Carola, Hernandez-Lain, Aurelio, Kornblum, Cornelia, Oldfors, Anders, Roach, Peter, Sandstedt, Joakim, Tasca, Giorgio, Thomsen, Christer, Visuttijai, Kittichate   +10 more
core   +1 more source

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

Biochemical characterization of digestive carbohydrases from Xanthogaleruca luteola and inhibition of its α-amylase by inhibitors extracted from the common bean [PDF]

, 2011
Xanthogaleruca luteola Müll. (Col.: Chrysomelidae) is a major urban insect pest on elm trees in Iran. Digestion in the alimentary canal of the elm leaf beetle is facilitated by some carbohydrases which are responsible for the digestion of ...
Ghadamyari Mohammad, Moghadam Mahdavi Maryam, Saiidi Fetemeh, Sharifi Mahbobeh   +3 more
core   +1 more source

Using Molecular Docking to Investigate the Alpha-amylase Inhibitory Activity of Bitter Peptides RK7 and KQ7 Derived from Yak Cheese [PDF]

Shipin Kexue, 2023
In this study, the physicochemical properties of two bitter peptides derived from yak cheese, RPKHPIK (RK7) and KVLPVPQ (KQ7) were calculated by using online bioinformatics tools such as ExPASy-ProtParam, Innovagen, and Pep-Draw.
LI Mengyao, LIANG Qi, SONG Xuemei
doaj   +1 more source