Activity of α-Amylase Inhibitors from Phaseolus coccineus on Digestive α-Amylases of the Coffee Berry Borer

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• 作者：Arnubio Valencia-Jim&#xe9 ; nez ; Jorge W. Arboleda Valencia ; Maria F&#xe1 ; tima Grossi-De-S&#xe1
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2008
• 出版时间：April 9, 2008
• 年：2008
• 卷：56
• 期：7
• 页码：2315 - 2320
• 全文大小：2094K
• 年卷期：v.56,no.7(April 9, 2008)
• ISSN：1520-5118

文摘

Seeds of scarlet runner bean (Phaseolus coccineus L.) were analyzed for α-amylase inhibitor (α-AI) activity. Through the use of polyclonal antibodies raised against pure α-AI-1 from common bean (Phaseolus vulgaris L.), typical α-ΑΙ polypeptides (M_r 14−18 kDa) as well as a large polypeptide of M_r 32000 Da, usually referred to as “amylase inhibitor like”, were detected. The inhibitor activity present in four accessions of P. coccineus was examined, both in semiquantitative zymograms allowing the separation of different isoforms and in quantitative assays against human salivary amylase, porcine pancreatic amylase, and coffee berry borer, Hypothenemus hampei Ferrari (Coleoptera: Scolytidae) amylase. Differential inhibition curves lead to the suggestion that the gene encoding one of the inhibitors in P. coccineus (in accession G35590) would be a good candidate for genetic engineering of coffee resistance toward the coffee berry borer. An in vitro proteolytic digestion treatment of pure α-ΑΙ-1 resulted in a rapid loss of the inhibitory activity, seriously affecting its natural capacity to interact with mammalian α-amylases.