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Amylase

About: Amylase is a research topic. Over the lifetime, 14164 publications have been published within this topic receiving 296069 citations.


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Journal ArticleDOI
TL;DR: A class of small polypeptides isolated from seeds of barley and millet has been found to have striking amino acid sequence identity with phospholipid transfer proteins, and the lack of any known activity for the barley protein suggests that the putative amylase inhibitors are lipid transfer proteins.

72 citations

Journal ArticleDOI
TL;DR: A modification of Somogyi's saccharogenic method for the determination of amylase activity has been presented for serum and urine as mentioned in this paper, where the starch substrate employed is buffered sufficiently to control the pH of sera and urines.
Abstract: A modification of Somogyi's saccharogenic method for the determination of amylase activity has been presented for serum and urine. The starch substrate employed is buffered sufficiently to control the pH of sera and urines. A study was made of the effect of varying enzyme and starch concentrations, pH, chloride and buffer concentrations, and temperature. Also studied were various starches and other substrates, several methods for quantitating reducing substances formed, stability of samples, precision, and normal values. Identification of intermediate and end products was made by paperchromatographic technics. Above a limiting concentration of starch, representing saturation of enzyme with substrate, a linear reaction rate was observed for a period of time that was found to be directly related to the initial starch concentration. Kjeldahl's law of proportionality has thus been confirmed for the ra-amylase activity of serum and urine. Evidence is presented that deviation from a linear reaction rate occurs at about the time the starch and high molecular weight dextrins no longer saturate the enzyme. Following this point, hydrolysis of lower molecular-weight sugars gradually becomes the preponderant reaction.

72 citations

Journal ArticleDOI
TL;DR: Structural-activity relationship was established through the interaction of the active compounds with enzyme active site with the help of docking studies, and all other analogs displayed good to moderate inhibitory potential.

72 citations

Journal ArticleDOI
TL;DR: Depending upon the composition of the medium and growth conditions, the fungus was found to secrete alpha- or beta-amylase, or both, and some of the properties of the partially purified alpha- amylase were found to be different from alpha-amymylases from other sources.
Abstract: The effect of different media and pH on the formation of amylase by Aspergillus oryzae EI 212 is described. Depending upon the composition of the medium and growth conditions, the fungus was found to secrete α- or β-amylase, or both. Some of the properties of the partially purified α-amylase were found to be different from α-amylases from other sources.

72 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20241
2023460
2022976
2021308
2020347
2019328