Covalent immobilization of a hydroperoxide lyase from mung beans (Phaseolus radiatus L.)

verfasst von: Bettina Rehbock, Ralf G. Berger
Abstract: A fatty acid hydroperoxide lyase of mung beans has been covalently immobilized on different commercially available gels which represents the first immobilization of this type of enzyme from a higher plant. UltraLink Iodoacetyl possessed optimum coupling properties and yielded a maximum activity of 1.3 U ml^-1 gel and a yield of 84%. The effect of various protective reagents (e.g. thiois, antioxidants) and of the substrate concentration on the re-usability of the immobilized enzyme was investigated. Compared to a control, the relative activity during re-use was enhanced 1.8-to 2.3-fold in the presence of dithiothreitol. As the hydroperoxide lyase was irreversibly inhibited by the substrate, its re-usability depended strongly on the hydroperoxide concentration. The lowest inactivation was with 55 μM hydroperoxide which resulted in a relative activity of 73% after the third cycle. The storage stability of the hydroperoxide lyase was significantly improved by immobilization and resulted in a relative activity of 86% after 18 days, whereas the soluble enzyme lost 68% of its initial activity.
Organisationseinheit(en): Institut für Lebensmittelchemie
Typ: Artikel
Journal: Biotechnology Techniques
Band: 12
Seiten: 539-544
Anzahl der Seiten: 6
ISSN: 0951-208X
Publikationsdatum: 07.1998
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Biochemie, Angewandte Mikrobiologie und Biotechnologie
Elektronische Version(en): https://doi.org/10.1023/A:1008855531469 (Zugang: Unbekannt)

BibTeX

@article{7b35c5b543224395b29004943d3f2eea,
title = "Covalent immobilization of a hydroperoxide lyase from mung beans (Phaseolus radiatus L.)",
abstract = "A fatty acid hydroperoxide lyase of mung beans has been covalently immobilized on different commercially available gels which represents the first immobilization of this type of enzyme from a higher plant. UltraLink Iodoacetyl possessed optimum coupling properties and yielded a maximum activity of 1.3 U ml-1 gel and a yield of 84%. The effect of various protective reagents (e.g. thiois, antioxidants) and of the substrate concentration on the re-usability of the immobilized enzyme was investigated. Compared to a control, the relative activity during re-use was enhanced 1.8-to 2.3-fold in the presence of dithiothreitol. As the hydroperoxide lyase was irreversibly inhibited by the substrate, its re-usability depended strongly on the hydroperoxide concentration. The lowest inactivation was with 55 μM hydroperoxide which resulted in a relative activity of 73% after the third cycle. The storage stability of the hydroperoxide lyase was significantly improved by immobilization and resulted in a relative activity of 86% after 18 days, whereas the soluble enzyme lost 68% of its initial activity.",
author = "Bettina Rehbock and Berger, {Ralf G.}",
note = "Funding information: This work was supported by the EU project AIR3-CT94-2060 and by the Fonds der Chemischen Industrie, Frankfurt.",
year = "1998",
month = jul,
doi = "10.1023/A:1008855531469",
language = "English",
volume = "12",
pages = "539--544",
journal = "Biotechnology Techniques",
issn = "0951-208X",
publisher = "Springer Netherlands",
number = "7",
}