Activation and Stabilization of Olive Recombinant 13-Hydroperoxide Lyase Using Selected Additives

Autor: Magali Mariani, Virginie Brunini-Bronzini de Caraffa, Jean Costa, Liliane Berti, Jean-Marie Desjobert, Alain Muselli, Claude Gambotti, Félix Tomi, Sophie Vincenti, Jacques Maury, S. Jacopini
Přispěvatelé: Laboratoire de Biochimie et Biologie Moléculaire Végétales - UMR6134, Université Pascal Paoli (UPP)-Centre National de la Recherche Scientifique (CNRS), Sciences pour l'environnement (SPE), Centre National de la Recherche Scientifique (CNRS)-Université Pascal Paoli (UPP), Laboratoire de Chimie des Produits Naturels -UMR 6134
Rok vydání: 2016
Předmět:
Zdroj: Applied Biochemistry and Biotechnology
Applied Biochemistry and Biotechnology, Humana Press, 2017, 182 (3), pp.1000-1013. ⟨10.1007/s12010-016-2377-0⟩
ISSN: 1559-0291
0273-2289
DOI: 10.1007/s12010-016-2377-0⟩
Popis: 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.
Databáze: OpenAIRE