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中国精品科技期刊2020
姚林锋, 何强. 单宁酸与胰α-淀粉酶作用特性研究[J]. 华体会体育, 2014, (03): 63-66. DOI: 10.13386/j.issn1002-0306.2014.03.040
引用本文: 姚林锋, 何强. 单宁酸与胰α-淀粉酶作用特性研究[J]. 华体会体育, 2014, (03): 63-66. DOI: 10.13386/j.issn1002-0306.2014.03.040
YAO Lin-feng, HE Qiang. Interaction between tannic acid and pancreatic α-amylase[J]. Science and Technology of Food Industry, 2014, (03): 63-66. DOI: 10.13386/j.issn1002-0306.2014.03.040
Citation: YAO Lin-feng, HE Qiang. Interaction between tannic acid and pancreatic α-amylase[J]. Science and Technology of Food Industry, 2014, (03): 63-66. DOI: 10.13386/j.issn1002-0306.2014.03.040

单宁酸与胰α-淀粉酶作用特性研究

Interaction between tannic acid and pancreatic α-amylase

  • 摘要: 本文考察了单宁酸对胰α-淀粉酶(PPA)的抑制作用,并通过紫外和荧光光谱法研究了二者的作用特性。研究发现单宁酸可明显抑制胰α-淀粉酶的活性,其作用类型为非竞争性抑制。单宁酸与胰α-淀粉酶的结合能自发进行,作用位点靠近PPA的色氨酸残基区域。二者结合后,可导致PPA在270nm附近的紫外吸收发生明显改变,并产生红移,同时可引起PPA荧光猝灭。 

     

    Abstract: The inhibitory effect on porcine pancreaticα- amylase ( PPA) and its inhibitory mechanism of tannic acid ( TA) was investigated by UV-vis absorption and fluorescent spectrometry.As a non-competitive inhibitor, tannic acid showed significant inhibitory effect on PPA.The TA- PPA interaction was a spontaneous molecular process, and the TA- PPA binding site was closer to PPA trytophan residues. The UV absorbance at 270nm of PPA decreased and the absorption bands showed red-shift when it interacted with tannic acid.In addition, the intrinsic fluorescence of PPA could be significantly quenched by tannic acid.

     

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