A novel dienelactone hydrolase from the thermoacidophilic archaeon Sulfolobus solfataricus P1: purification, characterization, and expression

Biochimica Et Biophysica Acta
Young-Jun ParkHee-Bong Lee

Abstract

Dienelactone hydrolases catalyze the hydrolysis of dienelactone to maleylacetate, which play a key role for the microbial degradation of chloroaromatics via chlorocatechols. Here, a thermostable dienelactone hydrolase from thermoacidophilic archaeon Sulfolobus solfataricus P1 was the first purified and characterized and then expressed in Escherichia coli. The enzyme was purified by using several column chromatographys and characterized by determining the enzyme activity using p-nitrophenyl caprylate and dienelactones. In addition, the amino acids related to the catalytic mechanism were examined by site-directed mutagenesis using the identified gene. The enzyme, approximately 29 kDa monomeric, showed the maximal activity at 74 degrees C and pH 5.0, respectively. The enzyme displayed remarkable thermostability: it retained approximately 50% of its activity after 50 h of incubation at 90 degrees C, and showed high stability against denaturing agents, including various detergents, urea, and organic solvents. The enzyme displayed substrate specificities toward trans-dienelactone, not cis-isomer, and also carboxylesterase activity toward p-nitrophenyl esters ranging from butyrate (C₄) to laurate (C₁₂). The k(cat)/K(m) ratios for tran...Continue Reading

Citations

May 21, 2013·Microbiological Research·Yanbing ZhuLuhong Hou
Jan 27, 2011·Biochemical Society Transactions·Patrick HaferkampBettina Siebers
May 22, 2018·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Joanna Perła-KajánHieronim Jakubowski
Sep 27, 2018·Archaea : an International Microbiological Journal·Mark James KrzmarzickAubrey Lynn McCutchan
Jul 18, 2018·Extremophiles : Life Under Extreme Conditions·Patricia S KumagaiAna P U Araujo
Mar 21, 2018·Extremophiles : Life Under Extreme Conditions·Noor Haza Fazlin HashimAbdul Munir Abdul Murad

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