Back to Search
Start Over
Improved recovery of active recombinant laccase from maize seed.
- Source :
-
Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2004 Jan; Vol. 63 (4), pp. 390-7. Date of Electronic Publication: 2003 Jun 12. - Publication Year :
- 2004
-
Abstract
- Lignolytic enzymes such as laccase have been difficult to over-express in an active form. This paper describes the expression, characterization, and application of a fungal laccase in maize seed. The transgenic seed contains immobilized and extractable laccase. Fifty ppm dry weight of aqueously extractable laccase was obtained, and the remaining solids contained a significant amount of immobilized laccase that was active. Although a portion of the extractable laccase was produced as inactive apoenzyme, laccase activity was recovered by treatment with copper and chloride. In addition to allowing the apoenzyme to regain activity, treatment with copper also provided a partial purification step by precipitating other endogenous corn proteins while leaving >90% of the laccase in solution. The data also demonstrate the application of maize-produced laccase as a polymerization agent. The apparent concentration of laccase in ground, defatted corn germ is approximately 0.20% of dry weight.
- Subjects :
- Apoenzymes isolation & purification
Apoenzymes metabolism
Chlorides metabolism
Copper metabolism
Fungal Proteins genetics
Laccase biosynthesis
Lignin metabolism
Plants, Genetically Modified enzymology
Plants, Genetically Modified genetics
Polyporales genetics
Recombinant Proteins biosynthesis
Recombinant Proteins genetics
Recombinant Proteins isolation & purification
Zea mays enzymology
Laccase genetics
Laccase isolation & purification
Polyporales enzymology
Seeds enzymology
Zea mays genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0175-7598
- Volume :
- 63
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Applied microbiology and biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 12802534
- Full Text :
- https://doi.org/10.1007/s00253-003-1362-z