Activity of hydroperoxide lyase under aqueous and micro-aqueous conditions

Jürgen-Lohmann, Dominik L.; Legge, Raymond L.

doi:10.1016/j.molcatb.2006.08.003

Cited by 3 publications

(1 citation statement)

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“…Unlike plant, E. coli, Y. lipolytica, and P. pastoris could produce only one hydroperoxide-metabolizing enzyme leading to the expected product. Furthermore, expressed versions of the enzyme from various sources resulted in much easier preparation and higher quantities of pure HPL [19].…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning, expression, and enzymatic characterization of Solanum tuberosum hydroperoxide lyase

Xue

Jiang

et al. 2012

Eur Food Res Technol

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A cDNA encoding hydroperoxide lyase (HPL) was isolated from Solanum tuberosum, cloned into pQE-30 vector, and expressed in E. coli. The recombinant protein was purified by nickel affinity chromatography and showed an approximate molecular weight of 54 kDa by SDS-PAGE analysis, which was similar to the predicted value based on the putative amino acid sequences (53.9 kDa). 13-Hydroperoxy-linolenic acid (13-HPOT) was the preferred substrate for the enzyme compared with 13-hydroperoxy-linoleic acid (13-HPOD). The corresponding volatile products were 2(E)-hexenal and n-hexanal tested by headspace-gas chromatography, respectively. The enzyme was optimally active at 25°C and pH 6.5. The K m , V max , and the catalytic efficiency (V max /K m ) for 13-HPOT were 56.6 lM, 71.3 units/mg, and 1.26 units/mg Á lM, respectively. Activity of the recombinant potato HPL increased when Triton X-100, sodium chloride, or potassium chloride was added in the reaction mixture, while calcium chloride decreased activity of the recombinant enzyme.

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Section: Introductionmentioning

confidence: 99%