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冬枣果实苯丙氨酸解氨酶酶学特性的研究

Characteristics of phenylalanine ammonia-lyase from Dongzao jujube fruit

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【作者】 丁薪源王睿袁树枝李丽莉王姣曹建康

【Author】 DING Xin-yuan;WANG Rui;YUAN Shu-zhi;LI Li-li;WANG Jiao;CAO Jian-kang;College of Food Science & Nutritional Engineering, China Agricultural University;

【机构】 中国农业大学食品科学与营养工程学院

【摘要】 研究了冬枣果实苯丙氨酸解氨酶(PAL)的酶学特性。L-苯丙氨酸为枣果实PAL的反应底物,结果表明,最适底物浓度为1.0 mmol/L。枣果实PAL属于别构酶,具有2个米氏常数,Km分别为0.115×10-4、8.177×10-4 mol/L。枣果实PAL最适温度为50℃,最适p H为8.8。在浓度为0~4.0 mmol/L范围里,L-半胱氨酸、酪氨酸、色氨酸、组氨酸均对枣果实PAL活性有一定的抑制作用,而抗坏血酸和蔗糖对PAL有激活作用。金属离子对PAL激活作用由强到弱依次为:Cu2+>Fe3+>Fe2+>Na+;金属离子对PAL抑制作用由强到弱依次为:Al3+>Mg2+>Mn2+>Ca2+>Zn2+>K+。研究结果揭示了冬枣果实PAL酶学特性,为通过调控枣果实PAL酶活性改善果实贮藏特性提供了理论依据。

【Abstract】 The characteristics of phenylalanine ammonia-lyase(PAL) in jujube fruit were studied. Results showed that the optimum concentration of the reaction substrate(L-phenylalanine) was identified to 1.0 mmol/L. PAL in jujube fruit was evidenced as a kind of allosteric enzyme that possesses two Michaelis constant. Values of Km were 0.115×10-4 mol/L and 8.177×10-4 mol/L. The optimum temperature for reaction of the enzyme was identified to 50 ℃, and the optimum p H was 8.8. In the concentration range from 0 mmol/L to 4.0 mmol/L, PAL activity was inhibited by the following agents: L-cysteine, tyrosine, tryptophan, and histidine, but was stimulated by ascorbic acid and sucrose. Some metal ions could activate the PAL activity, including(from strong to weak): Cu2+>Fe3+>Fe2+>Na+. Whereas, other metal ions that could inhibit the PAL activity were as the followings: Al3+>Mg2+>Mn2+>Ca2+>Zn2+>K+. The results revealed the characteristics of PAL in Dongzao jujube fruit and provided theoretical basis for improving fruit storage quality via the regulation of PAL activity of the jujube fruit.

【基金】 国家自然科学基金项目(31371846,31071625)
  • 【文献出处】 食品科技 ,Food Science and Technology , 编辑部邮箱 ,2015年02期
  • 【分类号】TS255.1
  • 【被引频次】12
  • 【下载频次】453
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