Results 11 to 20 of about 48,930 (267)
Expression ofAspergillus oryzaeα-amylase gene inSaccharomyces cerevisiae [PDF]
FEMS Microbiology Letters, 1993 Abstract A fragment containing the full length cDNA from Aspergillus oryzae α-amylase has been amplified by PCR using specific synthetic oligonucleotides. The amplified cDNA was designed to favour its expression in yeast by modifying its upstream untranslated region.
Francisca Randez-Gil, Pascual Sanz
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Encouragement of Enzyme Reaction Utilizing Heat Generation from Ferromagnetic Particles Subjected to an AC Magnetic Field. [PDF]
PLoS ONE, 2015 We propose a method of activating an enzyme utilizing heat generation from ferromagnetic particles under an ac magnetic field. We immobilize α-amylase on the surface of ferromagnetic particles and analyze its activity.
Masashi Suzuki +5 more
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Expression of theStreptomyces griseusα-amylase gene inEscherichia coli [PDF]
FEMS Microbiology Letters, 1994 The amy gene of Streptomyces griseus was not expressed in Escherichia coli cells due to the lack of recognition of the amy promoter by the E. coli RNA polymerase, as confirmed by using promoter-probe vectors. The expression of the amy gene in E. coli was detected only when the promoter-less gene was placed under the control of the lacZ promoter and was
T. Vigal, J.F. Martin, J.A. Gil
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Journal of Plant Protection Research, 2020 Plant derived α-amylase inhibitors are proteinaceous molecules that regulate the enzyme activity in plants and also protect plants from insect attack. In the current study, 28 accessions of 19 plant species were screened for their α-amylase inhibitory ...
Ashraf Oukasha Abd El-latif +3 more
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Journal of Enzyme Inhibition and Medicinal Chemistry, 2022 Different oleanolic acid (OA) oxime ester derivatives (3a-3t) were designed and synthesised to develop inhibitors against α-glucosidase and α-amylase. All the synthesised OA derivatives were evaluated against α-glucosidase and α-amylase in vitro.
Xu-Yang Deng +9 more
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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 +4 more
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Research progress on enhancement of bacterial α-amylase activity
Siliao yanjiu, 2023 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
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Molecular, Biochemical, and Dietary Regulation Features of α-Amylase in a Carnivorous Crustacean, the Spiny Lobster Panulirus argus. [PDF]
PLoS ONE, 2016 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
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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 +4 more
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Biota : Jurnal Ilmiah Ilmu-Ilmu Hayati, 2011 Penelitian ini bertujuan mengetahui karakter aktivitas immobilized amylase dan free amylase dari isolat amilolitik Zoogloea ramigera ABL 1 dengan beberapa kondisi lingkungan yang berbeda, seperti suhu, pH, temperatur, dan ion logam.
Endah Retnaningrum, Zukrotun Nafisah
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