Topic
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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TL;DR: In this article, the effects of polysaccharides in terms of displacing water and restricting gelatinisation with respect to the modified Flory-Huggins equation were investigated.
184 citations
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TL;DR: In this paper, a mixture of alpha-amylase and glucoamylases was used to hydrolyze granular starches to a variable degree at sub-gelatinization temperature, and produced a relatively high degree of conversion.
184 citations
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TL;DR: Production of d-lactic acid from rice bran, one of the most abundant agricultural by-products in Japan, is studied and the yield based on the amount of sugars soluble after 36-h hydrolysis of the bran by amylase and cellulase was 78%.
184 citations
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TL;DR: A 650-nucleotide cDNA from barley aleurone layers encoding a protein that is closely related to a known α-amylase inhibitor from Indian finger millet, and that has homologies to certain plant trypsin inhibitors is cloned and sequenced.
Abstract: We have cloned and sequenced a 650-nucleotide cDNA from barley (Hordeum vulgare L.) aleurone layers encoding a protein that is closely related to a known α-amylase inhibitor from Indian finger millet (Eleusine coracana Gaertn.), and that has homologies to certain plant trypsin inhibitors. mRNA for this probable amylase/protease inhibitor (PAPI) is expressed primarily in aleurone tissue during late development of the grain, as compared to that for the amylase/subtilisin inhibitor, which is expressed in endosperm during the peak of storage-protein synthesis. PAPI mRNA is present at high levels in aleurone tissue of desiccated, mature grain, and in incubated aleurone layers prepared from rehydrated mature seeds. Its expression in those layers is not affected by either abscisic acid or gibberellic acid, hormones that, respectively, increase and decrease the abundance of mRNA for the amylase/subtilisin inhibitor. PAPI mRNA is almost as abundant in gibberellic acid-treated aleurone layers as that for α-amylase, and PAPI protein is synthesized in that tissue at levels that are comparable to α-amylase. PAPI protein is secreted from aleurone layers into the incubation medium.
184 citations
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TL;DR: A family of three glycosylated acyl flavonols, montbretins A–C, was thereby identified and characterized as competitive amylase inhibitors, with Ki values ranging from 8.1–6100 nM, which suggest a binding mode for these inhibitors.
Abstract: Specific inhibitors of human pancreatic alpha-amylase (HPA) have potential as oral agents for the control of blood glucose levels in the treatment of diabetes and obesity. In a search for novel inhibitors, a library of 30 000 crude biological extracts of terrestrial and marine origin has been screened. A number of inhibitory extracts were identified, of which the most potent was subjected to bioassay-guided purification. A family of three glycosylated acyl flavonols, montbretins A-C, was thereby identified and characterized as competitive amylase inhibitors, with K(i) values ranging from 8.1-6100 nM. Competitive inhibition by myricetin, which corresponds to the flavone core, and noncompetitive inhibition by a second fragment, ethyl caffeiate, suggest a binding mode for these inhibitors.
184 citations