Details
| Original language | English |
|---|---|
| Pages (from-to) | 539-544 |
| Number of pages | 6 |
| Journal | Biotechnology Techniques |
| Volume | 12 |
| Issue number | 7 |
| Publication status | Published - Jul 1998 |
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.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Biotechnology Techniques, Vol. 12, No. 7, 07.1998, p. 539-544.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Covalent immobilization of a hydroperoxide lyase from mung beans (Phaseolus radiatus L.)
AU - Rehbock, Bettina
AU - Berger, Ralf G.
N1 - Funding information: This work was supported by the EU project AIR3-CT94-2060 and by the Fonds der Chemischen Industrie, Frankfurt.
PY - 1998/7
Y1 - 1998/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0031852379&partnerID=8YFLogxK
U2 - 10.1023/A:1008855531469
DO - 10.1023/A:1008855531469
M3 - Article
AN - SCOPUS:0031852379
VL - 12
SP - 539
EP - 544
JO - Biotechnology Techniques
JF - Biotechnology Techniques
SN - 0951-208X
IS - 7
ER -