一种高度耐热的噬菌体溶菌酶的鉴定与特性分析
Identification and characterization of a highly thermostable bacteriophage lysozyme.
作者信息
Lavigne R, Briers Y, Hertveldt K, Robben J, Volckaert G
机构信息
Laboratory of Gene Technology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, 3001 Leuven, Belgium.
出版信息
Cell Mol Life Sci. 2004 Nov;61(21):2753-9. doi: 10.1007/s00018-004-4301-y.
Abstract
Pseudomonas aeruginosa bacteriophage phiKMV is a T7-like lytic phage. Liquid chromatography-mass spectrometry of the structural proteins revealed gene product 36 (gp36) as part of the phiKMV phage particle. The presence of a lysozyme domain in the C terminal of this protein (gp36C) was verified by turbidimetric assays on chloroform-treated P. aeruginosa PAO1 and Escherichia coli WK6 cells. The molecular mass (20,884 Da) and pI (6.4) of recombinant gp36C were determined, as were the optimal enzymatic conditions (pH 6.0 in 16.7 mM phosphate buffer) and activity (4800 U/mg). Recombinant gp36C is a highly thermostable lysozyme, retaining 26% of its activity after 2 h at 100 degrees C and 21% after autoclaving. This thermostability could prove an interesting characteristic for food conservation technology.
摘要
铜绿假单胞菌噬菌体phiKMV是一种T7样裂解噬菌体。对结构蛋白进行液相色谱-质谱分析显示，基因产物36（gp36）是phiKMV噬菌体颗粒的一部分。通过对经氯仿处理的铜绿假单胞菌PAO1和大肠杆菌WK6细胞进行比浊法测定，证实了该蛋白（gp36C）的C末端存在溶菌酶结构域。测定了重组gp36C的分子量（20,884 Da）和pI（6.4），以及最佳酶促条件（在16.7 mM磷酸盐缓冲液中pH 6.0）和活性（4800 U/mg）。重组gp36C是一种高度耐热的溶菌酶，在100℃下2小时后保留其26%的活性，高压灭菌后保留21%的活性。这种热稳定性可能是食品保鲜技术的一个有趣特性。
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