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Activation and Stabilization of Olive Recombinant 13-Hydroperoxide Lyase Using Selected Additives.
Appl Biochem Biotechnol. 2017 Jul; 182(3):1000-1013.AB

Abstract

The stabilization of olive recombinant hydroperoxide lyases (rHPLs) was investigated using selected chemical additives. Two rHPLs were studied: HPL full-length and HPL with its chloroplast transit peptide deleted (matured HPL). Both olive rHPLs are relatively stable at 4 °C, and enzyme activity can be preserved (about 100% of the rHPL activities are maintained) during 5 weeks of storage at -20 or at -80 °C in the presence of glycerol (10%, v/v). Among the additives used in this study, glycine (2.5% w/v), NaCl (0.5 M), and Na2SO4 (0.25 M) provided the highest activation of HPL full-length activity, while the best matured HPL activity was obtained with Na2SO4 (0.25 M) and NaCl (1 M). Although the inactivation rate constants (k) showed that these additives inactivate both rHPLs, their use is still relevant as they strongly increase HPL activity. Results of C6-aldehyde production assays also showed that glycine, NaCl, and Na2SO4 are appropriate additives and that NaCl appears to be the best additive, at least for hexanal production.

Authors+Show Affiliations

Laboratoire de Biochimie et Biologie Moléculaire Végétales, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Laboratoire de Biochimie et Biologie Moléculaire Végétales, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Laboratoire de Biochimie et Biologie Moléculaire Végétales, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Laboratoire de Biochimie et Biologie Moléculaire Végétales, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Laboratoire de Biochimie et Biologie Moléculaire Végétales, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Laboratoire de Chimie des Produits Naturels, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Laboratoire de Chimie des Produits Naturels, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Laboratoire de Chimie des Produits Naturels, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Equipe Chimie et Biomasse, Université de Corse, CNRS UMR6134 SPE, Route des Sanguinaires, 20000, Ajaccio, France.Laboratoire de Biochimie et Biologie Moléculaire Végétales, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France.Laboratoire de Biochimie et Biologie Moléculaire Végétales, Université de Corse, CNRS UMR6134 SPE, Campus Grimaldi, BP52, 20250, Corte, France. maury@univ-corse.fr.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28013430

Citation

Jacopini, Sabrina, et al. "Activation and Stabilization of Olive Recombinant 13-Hydroperoxide Lyase Using Selected Additives." Applied Biochemistry and Biotechnology, vol. 182, no. 3, 2017, pp. 1000-1013.
Jacopini S, Vincenti S, Mariani M, et al. Activation and Stabilization of Olive Recombinant 13-Hydroperoxide Lyase Using Selected Additives. Appl Biochem Biotechnol. 2017;182(3):1000-1013.
Jacopini, S., Vincenti, S., Mariani, M., Brunini-Bronzini de Caraffa, V., Gambotti, C., Desjobert, J. M., Muselli, A., Costa, J., Tomi, F., Berti, L., & Maury, J. (2017). Activation and Stabilization of Olive Recombinant 13-Hydroperoxide Lyase Using Selected Additives. Applied Biochemistry and Biotechnology, 182(3), 1000-1013. https://doi.org/10.1007/s12010-016-2377-0
Jacopini S, et al. Activation and Stabilization of Olive Recombinant 13-Hydroperoxide Lyase Using Selected Additives. Appl Biochem Biotechnol. 2017;182(3):1000-1013. PubMed PMID: 28013430.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Activation and Stabilization of Olive Recombinant 13-Hydroperoxide Lyase Using Selected Additives. AU - Jacopini,Sabrina, AU - Vincenti,Sophie, AU - Mariani,Magali, AU - Brunini-Bronzini de Caraffa,Virginie, AU - Gambotti,Claude, AU - Desjobert,Jean-Marie, AU - Muselli,Alain, AU - Costa,Jean, AU - Tomi,Félix, AU - Berti,Liliane, AU - Maury,Jacques, Y1 - 2016/12/24/ PY - 2016/08/02/received PY - 2016/12/14/accepted PY - 2016/12/26/pubmed PY - 2017/6/27/medline PY - 2016/12/26/entrez KW - 3Z-hexenal KW - Additives KW - Green note KW - Hexanal KW - Hydroperoxide lyase KW - Stabilization SP - 1000 EP - 1013 JF - Applied biochemistry and biotechnology JO - Appl Biochem Biotechnol VL - 182 IS - 3 N2 - The stabilization of olive recombinant hydroperoxide lyases (rHPLs) was investigated using selected chemical additives. Two rHPLs were studied: HPL full-length and HPL with its chloroplast transit peptide deleted (matured HPL). Both olive rHPLs are relatively stable at 4 °C, and enzyme activity can be preserved (about 100% of the rHPL activities are maintained) during 5 weeks of storage at -20 or at -80 °C in the presence of glycerol (10%, v/v). Among the additives used in this study, glycine (2.5% w/v), NaCl (0.5 M), and Na2SO4 (0.25 M) provided the highest activation of HPL full-length activity, while the best matured HPL activity was obtained with Na2SO4 (0.25 M) and NaCl (1 M). Although the inactivation rate constants (k) showed that these additives inactivate both rHPLs, their use is still relevant as they strongly increase HPL activity. Results of C6-aldehyde production assays also showed that glycine, NaCl, and Na2SO4 are appropriate additives and that NaCl appears to be the best additive, at least for hexanal production. SN - 1559-0291 UR - https://www.unboundmedicine.com/medline/citation/28013430/Activation_and_Stabilization_of_Olive_Recombinant_13_Hydroperoxide_Lyase_Using_Selected_Additives_ DB - PRIME DP - Unbound Medicine ER -