乳酸乳球菌乳链菌蛋白酶III的自催化作用影响其对β-酪蛋白的特异性。
The autoproteolysis of Lactococcus lactis lactocepin III affects its specificity towards beta-casein.
作者信息
Flambard B, Juillard V
机构信息
Unité de Recherches Laitières et Génétique Appliquée, Institut National de la Recherche Agronomique, F-78350 Jouy-en-Josas, France.
出版信息
Appl Environ Microbiol. 2000 Dec;66(12):5134-40. doi: 10.1128/AEM.66.12.5134-5140.2000.
Abstract
The effect of autoproteolysis of Lactococcus lactis lactocepin III on its specificity towards beta-casein was investigated. beta-Casein degradation was performed by using either an autolysin-defective derivative of L. lactis MG1363 carrying the proteinase genes of L. lactis SK11, which was unable to transport oligopeptides, or autoproteolyzed enzyme purified from L. lactis SK11. Comparison of the peptide pools by high-performance liquid chromatography analysis revealed significant differences. To analyze these differences in more detail, the peptides released by the cell-anchored proteinase were identified by on-line coupling of liquid chromatography to mass spectrometry. More than 100 oligopeptides were released from beta-casein by the cell-anchored proteinase. Analysis of the cleavage sites indicated that the specificity of peptide bond cleavage by the cell-anchored proteinase differed significantly from that of the autoproteolyzed enzyme.
摘要
研究了乳酸乳球菌乳酸蛋白酶III的自催化作用对其β-酪蛋白特异性的影响。使用携带乳酸乳球菌SK11蛋白酶基因的乳酸乳球菌MG1363自溶素缺陷衍生物（其无法转运寡肽）或从乳酸乳球菌SK11纯化的自催化酶进行β-酪蛋白降解。通过高效液相色谱分析对肽库进行比较，结果显示存在显著差异。为了更详细地分析这些差异，通过液相色谱与质谱联用在线鉴定细胞锚定蛋白酶释放的肽。细胞锚定蛋白酶从β-酪蛋白中释放出100多种寡肽。对切割位点的分析表明，细胞锚定蛋白酶的肽键切割特异性与自催化酶的肽键切割特异性有显著差异。
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