Details
| Original language | English |
|---|---|
| Pages (from-to) | 55-60 |
| Number of pages | 6 |
| Journal | BBA - General Subjects |
| Volume | 1201 |
| Issue number | 1 |
| Publication status | Published - 28 Sept 1994 |
| Externally published | Yes |
Abstract
Commercial lipase (triacylglycerol lipase, EC 3.1.1.3) of Pseudomonas cepacia (Amano) has been purified to homogeneity by a single chromatography on phenyl Sepharose. The eluted lipase crystallized spontaneously at 4°C in the eluent, containing 58-69% 2-propanol. The yield of the lipase was 87-100% and the specific activity during the hydrolysis of triolein 5800 U/mg protein. This protein has a molecular weight of 34.1 kDa as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Its purity was determined by SDS-Page and capillary zone electrophoresis to be ≥ 99%. Immobilization on Sepharose increased its stability in organic solvents. This lipase of P. cepacia differs from that of other Pseudomonas strains in respect of substrate specificity and during crystallization. It exhibits a high stability in organic solvents and supercritical carbon dioxide.
Keywords
- (P. cepacia), Protein purification, Triacylglycerol lipase
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: BBA - General Subjects, Vol. 1201, No. 1, 28.09.1994, p. 55-60.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Lipase of Pseudomonas cepacia for biotechnological purposes: purification, crystallization and characterization
AU - Bornscheuer, Uwe
AU - Reif, Oscar Werner
AU - Lausch, Ralf
AU - Freitag, Ruth
AU - Scheper, Thomas
AU - Kolisis, Fragiskos N.
AU - Menge, Uldrich
N1 - Funding information: We are grateful to N. Tekkanat and K. Anastassiadis for technical assistance, and the European Communities for supporting the research in the framework of the BRIDGE-program (Grant BIOT-CT-90-0176).
PY - 1994/9/28
Y1 - 1994/9/28
N2 - Commercial lipase (triacylglycerol lipase, EC 3.1.1.3) of Pseudomonas cepacia (Amano) has been purified to homogeneity by a single chromatography on phenyl Sepharose. The eluted lipase crystallized spontaneously at 4°C in the eluent, containing 58-69% 2-propanol. The yield of the lipase was 87-100% and the specific activity during the hydrolysis of triolein 5800 U/mg protein. This protein has a molecular weight of 34.1 kDa as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Its purity was determined by SDS-Page and capillary zone electrophoresis to be ≥ 99%. Immobilization on Sepharose increased its stability in organic solvents. This lipase of P. cepacia differs from that of other Pseudomonas strains in respect of substrate specificity and during crystallization. It exhibits a high stability in organic solvents and supercritical carbon dioxide.
AB - Commercial lipase (triacylglycerol lipase, EC 3.1.1.3) of Pseudomonas cepacia (Amano) has been purified to homogeneity by a single chromatography on phenyl Sepharose. The eluted lipase crystallized spontaneously at 4°C in the eluent, containing 58-69% 2-propanol. The yield of the lipase was 87-100% and the specific activity during the hydrolysis of triolein 5800 U/mg protein. This protein has a molecular weight of 34.1 kDa as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Its purity was determined by SDS-Page and capillary zone electrophoresis to be ≥ 99%. Immobilization on Sepharose increased its stability in organic solvents. This lipase of P. cepacia differs from that of other Pseudomonas strains in respect of substrate specificity and during crystallization. It exhibits a high stability in organic solvents and supercritical carbon dioxide.
KW - (P. cepacia)
KW - Protein purification
KW - Triacylglycerol lipase
UR - http://www.scopus.com/inward/record.url?scp=0028111533&partnerID=8YFLogxK
U2 - 10.1016/0304-4165(94)90151-1
DO - 10.1016/0304-4165(94)90151-1
M3 - Article
C2 - 7522571
AN - SCOPUS:0028111533
VL - 1201
SP - 55
EP - 60
JO - BBA - General Subjects
JF - BBA - General Subjects
SN - 0304-4165
IS - 1
ER -