Interrelation of the Biosyntheses of Lipids, Lipoxygenase, and Lipase in Cultured Streptomycetes

Popova, N. N.; Krivova, А. Yu.; Rastimeshina, I. O.; Burtseva, S. A.

doi:10.1007/s11021-005-0114-8

Cited by 1 publication

(3 citation statements)

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“…While build-up of TAGs is common among eukaryotes and some prokaryotes, the saturated, odd-numbered carbon chain TAGs of S. coelicolor are unique in composition [16] . Their metabolism is associated with inherent but yet uncharacterized lipolytic activity [15] , [18] . Herein we focus on the characterization of the intracellular esterase EstC from S. coelicolor , an enzyme displaying promising activity for cold-adapted industrial processes.…”

Section: Resultsmentioning

confidence: 99%

“…As a result, it is not surprising that ubiquitous lipolytic activity can be found among streptomycetes [10] – [14] . Some reports also show that streptomycetes such as Streptomyces coelicolor and the closely related specie Streptomyces lividans are capable of important accumulations of cytoplasmic triacylglycerols (TAGs) in the stationary phase [15] – [18] . It was presumed that the build-up of TAGs could serve as a carbon source for the synthesis of polyketide antibiotics in nutrient depletion situations [15] , [19] , [20] .…”

Section: Introductionmentioning

confidence: 99%

“…While the accumulation of TAGs is a common feature among actinomycetes, streptomycetes differ in the accumulation of neutral lipids of rare types, such as iso- and anteiso- ramified TAGs with odd carbon chains (13, 15 and 17 carbons) [17] , [19] . Furthermore, this accumulation of TAGs was recently correlated to the activation of lipolytic activity [15] , [18] , but the characterization of lipolytic enzymes implicated in such activity remains elusive [17] , [21] .…”

Section: Introductionmentioning

confidence: 99%

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Isolation and Characterization of EstC, a New Cold-Active Esterase from Streptomyces coelicolor A3(2)

et al. 2012

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The genome sequence of Streptomyces coelicolor A3(2) contains more than 50 genes coding for putative lipolytic enzymes. Many studies have shown the capacity of this actinomycete to store important reserves of intracellular triacylglycerols in nutrient depletion situations. In the present study, we used genome mining of S. coelicolor to identify genes coding for putative, non-secreted esterases/lipases. Two genes were cloned and successfully overexpressed in E. coli as His-tagged fusion proteins. One of the recombinant enzymes, EstC, showed interesting cold-active esterase activity with a strong potential for the production of valuable esters. The purified enzyme displayed optimal activity at 35°C and was cold-active with retention of 25% relative activity at 10°C. Its optimal pH was 8.5–9 but the enzyme kept more than 75% of its maximal activity between pH 7.5 and 10. EstC also showed remarkable tolerance over a wide range of pH values, retaining almost full residual activity between pH 6–11. The enzyme was active toward short-chain p-nitrophenyl esters (C2–C12), displaying optimal activity with the valerate (C5) ester (k cat/K m = 737±77 s−1 mM−1). The enzyme was also very active toward short chain triglycerides such as triacetin (C2:0) and tributyrin (C4:0), in addition to showing good primary alcohol and organic solvent tolerance, suggesting it could function as an interesting candidate for organic synthesis of short-chain esters such as flavors.

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Section: Resultsmentioning

confidence: 99%