Production of dipeptidyl peptidase IV inhibitory peptides from defatted rice bran

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• 作者：Tadashi Hatanaka^a ; ^{hatanaka@bio-ribs.com} ; Yosikazu Inoue^b ; Jiro Arima^c ; Yuya Kumagai^a ; Hirokazu Usuki^a ; ^d ; Kayoko Kawakami^a ; Masayo Kimura^a ; Takafumi Mukaihara^a
• 关键词：DPP-IV ; dipeptidyl peptidase IV ; GLP-1 ; glucagon-like peptide-1 ; HPLC ; high-performance liquid chromatography ; IC50 ; half-maximal inhibitory concentration ; LAP ; leucine aminopeptidase ; LC&ndash ; MS ; HPLC&ndash ; mass spectrometry ; pNA ; p-nitroanilide ; RB ; ri
• 刊名：Food Chemistry
• 出版年：2012
• 期刊代码：48_03088146
• 类别：abs
• 出版时间：15 September, 2012
• 卷：134
• 期：2
• 页码：797-802
• 文件大小：459 K

摘要

The insulinotropic hormone glucagon-like peptide-1 is metabolised extremely rapidly by the ubiquitous enzyme dipeptidyl peptidase IV (DPP-IV). Therefore, human DPP-IV is a key regulator involved in the prevention and treatment of type 2 diabetes. To simplify the method of producing an inhibitory peptide against DPP-IV, we focused on rice bran (RB) as a source and subjected proteins from defatted RB to enzymatic proteolysis using 2 commercial enzymes. The RB peptides produced with Umamizyme G exhibited 10 times the inhibitory activity as those produced with Bioprase SP. The half-maximal inhibitory concentration (IC₅₀) value of the RB peptides was 2.3 卤 0.1 mg/ml. Leu-Pro and Ile-Pro were identified as the inhibitory peptides among the RB peptides produced with Umamizyme G. Ile-Pro was the strongest DPP-IV inhibitor among the 15 Xaa-Pro dipeptides and Pro-Ile tested. Ile-Pro competitively inhibited DPP-IV (K_i = 0.11 mM). Mass spectrometry indicated that the contents of Leu-Pro and Ile-Pro in the RB peptides were 2.91 卤 0.52 渭g/mg.