Novel cholesterol esterase secreted by Streptomyces persists during aqueous long-term storage

Journal of Bioscience and Bioengineering
Hongyu XiangTakayuki Hoshino

Abstract

We isolated a moderate thermophilic actinomycete, Streptomyces sp. X9, from soil and purified cholesterol esterase (CHE) from the culture medium to homogeneity. The molecular masses of the purified CHE estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration chromatography were 23.6 and 163 kDa, respectively, indicating that the enzyme assumes an oligomeric form. Heavy metals such as Hg2+ and Ag+ similarly inhibited the activity of the CHE in the same manner as those of other bacterial CHEs. The activity of Streptomyces sp. X9 CHE was susceptible to dithiothreitol, beta-mercaptoethanol and p-chloromercuribenzoate, but resistant to phenylmethylsulfonyl fluoride, unlike those of other bacterial CHEs. The purified CHE could utilize both cholesteryl and p-nitrophenyl (pNP) esters of fatty acids as substrates. Steady-state kinetics revealed respective Km values for cholesteryl myristate and pNP-myristate of 0.34 and 1.1 mM, indicating that the cholesteryl residue is important for catalysis. We also found that the Km for the pNP esters are dependent on the chain length of the substrate fatty acid residues. These results indicate that the novel CHE specifically hydrolyzes substrates by recognizing both...Continue Reading

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Citations

Jun 9, 2012·Microbial Cell Factories·Víctor Barba CedilloMaría Jesús Martínez
Jan 9, 2016·Applied Microbiology and Biotechnology·Maria Eugenia VaqueroAlicia Prieto
Dec 13, 2006·Biochimica Et Biophysica Acta·Hongyu XiangNaoki Takaya
May 24, 2008·Journal of Bioscience and Bioengineering·Atsushi MaedaAkio Sugihara
Sep 27, 2018·Future Microbiology·Nagender Rao RameshwaramSangita Mukhopadhyay

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