火鸡肌肉丙氨酰氨肽酶的酶学特性  

Enzymatic Characterization of Alanine Aminopeptidase from Turkey Skeletal Muscle

作　　者：田甜[1] 魏延玲[1] 何立超[1] 阮贵萍 张迎阳[1] 章建浩[1] 

机构地区：[1]国家肉品质量安全控制工程技术研究中心,教育部肉品加工与质量控制重点实验室,农业部农畜产品加工与质量控制重点开放实验室,南京农业大学食品科技学院,江苏南京210095

出　　处：《食品科学》2013年第9期205-209,共5页Food Science

基　　金：江苏高校优势学科建设工程资助项目;“十二五”国家科技支撑计划项目(2012BAD28B01)

摘　　要：通过45%～65%的硫酸铵沉淀法,从火鸡肌肉中分离得到初步纯化的丙氨酰氨肽酶(AAP,EC 3.4.11.14),研究其酶学特性及盐分和AAP水解产物对其酶活力的影响。结果表明:AAP的最适反应温度为37～39℃,最适pH值约为6.8～7.5。0.8mol/L的NaCl仅抑制10%的AAP相对酶活力,说明盐分对AAP的酶活力抑制作用较弱;AAP主要水解产物丙氨酸(Ala)对AAP几乎没有抑制作用,而其他产物氨基酸均对AAP有较显著的反馈抑制作用(P<0.05),对AAP的抑制作用强弱顺序为苯丙氨酸>赖氨酸>亮氨酸>甲硫氨酸。An alanine aminopeptidase（AAP,EC 3.4.11.14） was purified from turkey skeletal muscle by using 45%—65% ammonium sulphate fractionation,its enzymatic properties and the effect of salt and its hydrolysis products on enzyme activity was studied.The results showed that optimal reaction temperature of AAP was 37—39 ℃,and the optimal pH was approximately 6.8—7.5.In addition,0.8 mol/L NaCl revealed the inhibition on the activity of AAP by 10% so that salt had a weakly inhibitory function to AAP activity.Alanine（Ala）,as the major hydrolysis product,almost had no inhibitory effect on AAP,while the other amino acids had significant feedback inhibition（P ＆lt; 0.05） on AAP.We found that 100 mmol/L phenylalanine（Phe）,lysine（Lys）,leucine（Leu） and methionine（Met） could inhibit the activity of AAP,and the sequence of inhibitory is Phe ＆gt; Lys ＆gt; Leu ＆gt; Met.

关 键 词：火鸡 丙氨酰氨肽酶 盐分 氨基酸 反馈抑制 

分 类 号：Q814.1[生物学—生物工程]