Production, Purification and Characterization of the Hen Egg- White Lysozyme Inhibitor from Enterobacter cloacae M-1002

doi:10.1002/jccs.199700052

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Title:	Production, Purification and Characterization of the Hen Egg- White Lysozyme Inhibitor from Enterobacter cloacae M-1002
Authors:	王三郎;Wang, S. L.;白其昇;Pai, C. S.;謝順堂;Shieh, S. T.
Contributors:	淡江大學生命科學研究所
Keywords:	Lysozyme;Lysozyme Inhibitor;Antibiotics;Enterobacter Cloacae 溶菌；溶菌抑制劑；抗生素；共泄腔腸桿菌
Date:	1997-06-01
Issue Date:	2013-07-11 11:25:44 (UTC+8)
Publisher:	臺北市：中國化學學會
Abstract:	Three hen egg-white lysozyme inhibitor producing strains, Enterobacter cloacae M-1002, E. sakazakii M-1204, and Erwinia rhapontici H-55, were isolated from the soils of Taiwan. E. cloacae M-1002 appeared to be a promising inhibitor producing strain. One inhibitor was isolated from the culture broth of this strain. Maximum lysozyme inhibitory activity was obtained when the bacterium was grown aerobically in a medium consisting of 0.75% glucose, 0.25% beef extract, 1.0% polypeptone, and 0.25% sodium L- glutamate (pH 7.0) at 37.degree.C after 36-48 hrs. A hen egg-white lysozyme inhibitor was isolated from the culture broth of this strain. The inhibitor was purified from the culture supernatant of E. cloacae M-1002 by ammonium sulfate fractionation, DEAE-Sepharose CL-6B column chromatography and Fractogel TSK HW-55 (S) gel chromatography. Molecular weight of the purified lysozyme inhibitor was estimated to be 18,000-20,000 by SDS-PAGE and HPLC, and was composed of 71% amino acid and 23% total sugar. Serine, glycine, and alanine in a 3:2:1 molar ratio were the major amino acids, calculated to be 32.8, 20.3, and 11.4% (mol%), respectively. Glucose and mannose were the major sugar components of the inhibitor. The inhibitor was stable at pH 5 to 8 and was stable under 50.degree.C. Only hen egg-white lysozyme was inhibited by the purified inhibitor but not the other tested enzymes such as lysozyme of celery, turnip; lytic enzyme of Pseudomonas aeruginosa M- 1001; chitinase/ lysozyme of P. aeruginosa K-187; or cellulase and xylanase of Streptomyces actuosus A-151 and Aspergillus sp. G-393. The inhibition of lysozyme to the bacterial cell lytic activity by the purified inhibitor was 100%.
Relation:	Journal of the Chinese Chemical Society=中國化學會會誌 44(3), pp.349-355
DOI:	10.1002/jccs.199700052
Appears in Collections:	[Graduate Institute & Department of Chemistry] Journal Article

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