摘要
为了实现鲎素这种高效、广谱的抗菌肽在生产实践中的应用,采用不同温度、pH值、体外蛋白酶（胃蛋白酶、胰蛋白酶、弹性蛋白酶、羧肽酶B）分别处理鲎素,通过检测鲎素最小抑菌浓度（M IC）的变化来衡量鲎素的生物活性稳定性;采用高效液相色谱（HPLC）检测鲎素残留量,通过HPLC图谱变化来评定鲎素分子结构的稳定性.结果表明：温度小于120℃、pH值小于11.30时,鲎素对大肠杆菌K88的M IC为1.25～5.00mg/L;高效液相色谱检测得鲎素残留量在65.46～70.21μg之间;鲎素对胃蛋白酶的作用表现出很高的稳定性,对胰蛋白酶、羧肽酶B、弹性蛋白酶的作用稍微敏感;在胃蛋白酶酶活浓度不高于5.33mmol/（s.L）、胰蛋白酶酶活浓度不高于0.67mmol/（s.L）、羧肽酶B酶活浓度不高于0.17mmol/（s.L）、弹性蛋白酶酶活浓度不高于0.021mmol/（s.L）的条件下,鲎素仍具有活性.这说明鲎素抗菌肽具有较强的高温耐受性,在酸性条件下具有稳定性,且具有一定的耐受蛋白酶降解的能力.
In order to apply tachyplesin, a high-perforvaance and broad-spectrum antibacterial peptide to the pharmaceutical industry, the biological stability of tachyplesin varying with the temperature, the pH value and the proteinases such as trypsin, pepsin, elastase and caboxypeptidase B was investigated and was described by the minimal inhibitory concentration （ MIC ）. Moreover, the stability of molecular structure was evaluated by the peak change in high-performance liquid chromatography （HPLC）. The results indicate that （1） at 120℃, when the pH value reaches 11.30, the MIC of tachyplesin against E. Coli K88 ranges from 1.25 to 5.0 mg/L and the residual content of tachyplesin detected by HPLC varies from 65. 46 to 70. 21 μg; （2） tachyplesin is sensitive to trypsin, carboxypeptidase B and elastase, but remains stable with pepsin; and （3） tachyplesin is stable in the solution with the pepsin, trypsin carboxypeptidase B and elastase contents of not more than 5. 33 mmol/（ s· L）, 0. 33 mmol/（ s · L ）, 0. 17 mmol/（ s·L） and 0. 021 mmol/（s · L）, respectively. It is thus concluded that tachyplesin is of high heat resistance, good stability and excellent anti-enzymatic degradability.
出处
《华南理工大学学报（自然科学版）》
EI
CAS
CSCD
北大核心
2008年第4期144-150,共7页
Journal of South China University of Technology(Natural Science Edition)
基金
广东省自然科学基金资助项目(05300281,04011209)
广东省“千百十工程”人才培养专项基金项目(0326403,0326402)
深圳市科技计划资助项目(05KJBB003)
关键词
鲎素
抗菌肽
蛋白酶
抗菌活性
分子结构
结构稳定性
tachyplesin
antibacterial peptide
proteinase
antibacterial activity
molecular structure
structure stability
