摘要
研究了温度、pH、干燥方式和体外肠道酶消化对蚕蛹源ACE抑制肽稳定性的影响,并通过Lineweaver-Burk双倒数曲线作图和紫外光谱初步探讨了蚕蛹源ACE抑制肽对ACE的抑制机理。结果表明:蚕蛹源ACE抑制肽在高温、酸性和碱性条件下不稳定,易失活;冷冻干燥和喷雾干燥对蚕蛹源ACE抑制肽的活性影响较小;蚕蛹源ACE抑制肽对胃蛋白酶、胰蛋白酶和α-胰凝乳蛋白酶具有较强的抗消化能力,经胃蛋白酶、胰蛋白酶和α-胰凝乳蛋白酶共同消化后,蚕蛹源ACE抑制肽仍能保留初始活性的94.0%;蚕蛹源ACE抑制肽竞争性抑制ACE,其抑制常数(Ki)为0.06 mg/mL;ACE被蚕蛹源ACE抑制肽抑制后,ACE在240～280 nm附近的紫外吸光值明显增加,初步揭示了蚕蛹源ACE抑制肽抑制ACE活性时,ACE的分子结构发生了改变。
Effects of temperature,pH,drying methods and in vitro digestion of intestinal enzyme on the stabilities of angiotensin-Ⅰ converting enzyme （ACE） inhibitory peptides from silkworm pupae were studied.Furthermore,the inhibitory mechanism of ACE-inhibitory peptides from silkworm pupae against ACE was preliminarily studied based on the analyses of Lineweaver-Burk plots and ultraviolet spectrum.The results showed that,ACE-inhibitory peptides from silkworm pupae were instability and easy inactivation under the conditions of high temperature,acidic or alkaline.The effects of freeze-drying and spray-drying on the peptides activity were smaller.The peptides were resistant to digestion by pepsin,trypsin and α-chymotrypsin.After co-digestion by pepsin,trypsin and α-chymotrypsin,the peptides activity could maintain 94.0% of their initial activity.Moreover,the inhibition pattern against ACE revealed that the peptides were competitive inhibitors with inhibition constants（Ki） 0.06 mg/mL.After the inhibition by the peptides,the ultraviolet absorbance values of ACE at 240～280 nm were significant increase,and these changes of ultraviolet absorbance values initially revealed that ACE molecular structure has been changed.
出处
《食品与生物技术学报》
CAS
CSCD
北大核心
2013年第8期875-881,共7页
Journal of Food Science and Biotechnology
基金
江苏省自然科学基金项目(BK2012693)
关键词
蚕蛹
ACE抑制肽
稳定性
抑制
ACE动力学
silkworm pupae
angiotensin-Ⅰ converting enzyme （ACE） inhibitory peptides
stabilities
inhibition
ACE kinetics
