https://scholars.lib.ntu.edu.tw/handle/123456789/377907
Title: | Inhibitory potential of fatty acids on key enzymes related to type 2 diabetes | Authors: | Su, C.-H. CHUN-HUA HSU Ng, L.-T. LEAN-TEIK HUANG |
Keywords: | α-amylase; α-glucosidase; Fatty acids; Linoleic acid; Oleic acid; Type 2 diabetes | Issue Date: | 2013 | Journal Volume: | 39 | Journal Issue: | 4 | Start page/Pages: | 415-421 | Source: | BioFactors | Abstract: | This study aimed to examine the inhibitory mechanisms of fatty acids on key enzymes related to type 2 diabetes, and their effects on starch digestion rate. Among the 10 fatty acids analyzed, oleic acid showed the strongest anti-α-glucosidase activity, followed by linoleic acid, and their activities were more potent than acarbose, but they possessed a weaker anti-α-amylase activity. Kinetic assays demonstrated that oleic acid and linoleic acid were competitive inhibitors, and their interactions with α-glucosidase exhibited a character of static quenching, which indicates that they would bind to α-glucosidase to form a complex. However, they had little effects on the secondary structures of α-glucosidase. In vitro study showed that oleic acid and linoleic acid were more potent than acarbose in inhibiting starch digestion. Taken together, these results conclude that oleic acid and linoleic acid possess potent inhibitory effects on α-glucosidase activity. ? 2013 International Union of Biochemistry and Molecular Biology, Inc. |
URI: | http://www.scopus.com/inward/record.url?eid=2-s2.0-84881667117&partnerID=MN8TOARS http://scholars.lib.ntu.edu.tw/handle/123456789/377907 |
DOI: | 10.1002/biof.1082 | SDG/Keyword: | amylase; arachidonic acid; decanoic acid; fatty acid; glucosidase; lauric acid; linoleic acid; linolenic acid; myristic acid; oleic acid; palmitic acid; palmitoleic acid; starch; stearic acid; alpha glucosidase; antidiabetic agent; fatty acid; glycosidase inhibitor; article; controlled study; drug effect; enzyme inhibition; non insulin dependent diabetes mellitus; priority journal; antagonists and inhibitors; chemistry; circular dichroism; Diabetes Mellitus, Type 2; enzymology; human; hydrolysis; kinetics; protein secondary structure; alpha-Amylases; alpha-Glucosidases; Circular Dichroism; Diabetes Mellitus, Type 2; Fatty Acids; Glycoside Hydrolase Inhibitors; Humans; Hydrolysis; Hypoglycemic Agents; Kinetics; Protein Structure, Secondary; Starch |
Appears in Collections: | 農業化學系 |
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