Purification and characterization of two distinct lipases from Candida cylindracea
We have purified and characterized two isoenzymes from a commercial lipase preparation of Candida cylindracea. The purification procedure includes ethanol precipitation and DEAE-Sephacel and Sephacryl HR 100 chromatographies. Lipase A and lipase B were purified 11-fold with a 5% and 21% recovery in...
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| Published in | Biochimica et biophysica acta Vol. 1156; no. 2; pp. 181 - 189 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Amsterdam
Elsevier B.V
13.02.1993
Elsevier |
| Subjects | |
| Online Access | Get full text |
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| Abstract | We have purified and characterized two isoenzymes from a commercial lipase preparation of
Candida cylindracea. The purification procedure includes ethanol precipitation and DEAE-Sephacel and Sephacryl HR 100 chromatographies. Lipase A and lipase B were purified 11-fold with a 5% and 21% recovery in activity, respectively. The enzymes have similar amino acid content, N-terminal sequence and molecular weight, but differ on neutral sugar content, hydrophobicity, presence of isoforms and stability to pH and temperature. They also show some differences in the substrate specificity. |
|---|---|
| AbstractList | We have purified and characterized two isoenzymes from a commercial lipase preparation of
Candida cylindracea. The purification procedure includes ethanol precipitation and DEAE-Sephacel and Sephacryl HR 100 chromatographies. Lipase A and lipase B were purified 11-fold with a 5% and 21% recovery in activity, respectively. The enzymes have similar amino acid content, N-terminal sequence and molecular weight, but differ on neutral sugar content, hydrophobicity, presence of isoforms and stability to pH and temperature. They also show some differences in the substrate specificity. We have purified and characterized two isoenzymes from a commercial lipase preparation of Candida cylindracea. The purification procedure includes ethanol precipitation and DEAE-Sephacel and Sephacryl HR 100 chromatographies. Lipase A and lipase B were purified 11-fold with a 5% and 21% recovery in activity, respectively. The enzymes have similar amino acid content, N-terminal sequence and molecular weight, but differ on neutral sugar content, hydrophobicity, presence of isoforms and stability to pH and temperature. They also show some differences in the substrate specificity. We have purified and characterized two isoenzymes from a commercial lipase preparation of Candida cylindracea . Lipase A and lipase B have similar amino acid content, N-terminal sequence and molecular weight, but differ on neutral sugar content. We have purified and characterized two isoenzymes from a commercial lipase preparation of Candida cylindracea. The purification procedure includes ethanol precipitation and DEAE-Sephacel and Sephacryl HR 100 chromatographies. Lipase A and lipase B were purified 11-fold with a 5% and 21% recovery in activity, respectively. The enzymes have similar amino acid content, N-terminal sequence and molecular weight, but differ on neutral sugar content, hydrophobicity, presence of isoforms and stability to pH and temperature. They also show some differences in the substrate specificity.We have purified and characterized two isoenzymes from a commercial lipase preparation of Candida cylindracea. The purification procedure includes ethanol precipitation and DEAE-Sephacel and Sephacryl HR 100 chromatographies. Lipase A and lipase B were purified 11-fold with a 5% and 21% recovery in activity, respectively. The enzymes have similar amino acid content, N-terminal sequence and molecular weight, but differ on neutral sugar content, hydrophobicity, presence of isoforms and stability to pH and temperature. They also show some differences in the substrate specificity. |
| Author | Díaz-Mauriño, Teresa Ballesteros, Antonio Fernández, Victor M. Otero, Cristina Rúa, M.Luisa |
| Author_xml | – sequence: 1 givenname: M.Luisa surname: Rúa fullname: Rúa, M.Luisa organization: Instituto de Catálisis, CSIC, Universidad Autónoma, Madrid Spain – sequence: 2 givenname: Teresa surname: Díaz-Mauriño fullname: Díaz-Mauriño, Teresa organization: Instituto de Química-Física ‘Rocasolano’, CSIC, Madrid Spain – sequence: 3 givenname: Victor M. surname: Fernández fullname: Fernández, Victor M. organization: Instituto de Catálisis, CSIC, Universidad Autónoma, Madrid Spain – sequence: 4 givenname: Cristina surname: Otero fullname: Otero, Cristina organization: Instituto de Catálisis, CSIC, Universidad Autónoma, Madrid Spain – sequence: 5 givenname: Antonio surname: Ballesteros fullname: Ballesteros, Antonio organization: Instituto de Catálisis, CSIC, Universidad Autónoma, Madrid Spain |
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| Keywords | Candida cylindracea Bes THF Enzyme purification Con A Isoenzyme Mes Lipase Candida rugosa Enzyme characterization Fungi Purification Enzymatic activity Enzyme Substrate specificity Triacylglycerol lipase Fungi Imperfecti Physicochemical properties Aminoacid sequence Thallophyta |
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| Snippet | We have purified and characterized two isoenzymes from a commercial lipase preparation of
Candida cylindracea. The purification procedure includes ethanol... We have purified and characterized two isoenzymes from a commercial lipase preparation of Candida cylindracea. The purification procedure includes ethanol... We have purified and characterized two isoenzymes from a commercial lipase preparation of Candida cylindracea . Lipase A and lipase B have similar amino acid... |
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| StartPage | 181 |
| SubjectTerms | Amino Acid Sequence Amino Acids - analysis Biological and medical sciences Candida - enzymology Candida cylindracea Candida rugosa Enzyme characterization Enzyme purification Fundamental and applied biological sciences. Psychology Growth, nutrition, metabolism, transports, enzymes. Molecular biology Hot Temperature Hydrogen-Ion Concentration Isoenzyme Isoenzymes - chemistry Isoenzymes - isolation & purification Kinetics Lipase Lipase - chemistry Lipase - isolation & purification Microbiology Molecular Sequence Data Molecular Weight Mycology Solvents Substrate Specificity Temperature Triolein - metabolism |
| Title | Purification and characterization of two distinct lipases from Candida cylindracea |
| URI | https://dx.doi.org/10.1016/0304-4165(93)90134-T https://www.ncbi.nlm.nih.gov/pubmed/8427877 https://www.proquest.com/docview/16515810 https://www.proquest.com/docview/75569637 |
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