Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris: High-level production and some properties of functional expressed lipase B

E. Catoni; C. Schmidt-Dannert; S. Brocca; R. D. Schmid

doi:10.1023/A:1018419729009

Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris: High-level production and some properties of functional expressed lipase B

E. Catoni, C. Schmidt-Dannert, S. Brocca, R. D. Schmid

Biochemistry, Molecular Biology, and Biophysics (CBS)

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36 Scopus citations

Abstract

Lipase A and B from Geotrichum candidum CMICC 335426 were functionally expressed and secreted in Pichia pastoris. Lipase B exhibits a unique substrate specificity for long-chain cis-Δ9 unsaturated triacylglycerols. Thus, using different cultivation conditions, the production of recombinant lipase B was optimised, yielding 200 000 Units per liter culture. After overexpression lipase B was purified by diafiltration (372 U/mg). The investigated enzyme properties were comparable to those reported for the native enzyme.

Original language	English (US)
Pages (from-to)	689-695
Number of pages	7
Journal	Biotechnology Techniques
Volume	11
Issue number	9
DOIs	https://doi.org/10.1023/A:1018419729009
State	Published - 1997

Bibliographical note

Funding Information:
We would like to thank Eckart Bonacker for performing the cultivations and for his technical assistance. We thank Dr. Chris Davies (Unilever, Colworth House) for providing us the lipases genes. Elisabetta Catoni gratefully acknowledges a scholarship from the European Commision as part of an European Community Training Project (BIO4-CT96–5059, ΔG12-SSMA).

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title = "Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris: High-level production and some properties of functional expressed lipase B",

abstract = "Lipase A and B from Geotrichum candidum CMICC 335426 were functionally expressed and secreted in Pichia pastoris. Lipase B exhibits a unique substrate specificity for long-chain cis-Δ9 unsaturated triacylglycerols. Thus, using different cultivation conditions, the production of recombinant lipase B was optimised, yielding 200 000 Units per liter culture. After overexpression lipase B was purified by diafiltration (372 U/mg). The investigated enzyme properties were comparable to those reported for the native enzyme.",

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doi = "10.1023/A:1018419729009",

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AU - Schmidt-Dannert, C.

AU - Brocca, S.

AU - Schmid, R. D.

N1 - Funding Information: We would like to thank Eckart Bonacker for performing the cultivations and for his technical assistance. We thank Dr. Chris Davies (Unilever, Colworth House) for providing us the lipases genes. Elisabetta Catoni gratefully acknowledges a scholarship from the European Commision as part of an European Community Training Project (BIO4-CT96–5059, ΔG12-SSMA).

PY - 1997

Y1 - 1997

N2 - Lipase A and B from Geotrichum candidum CMICC 335426 were functionally expressed and secreted in Pichia pastoris. Lipase B exhibits a unique substrate specificity for long-chain cis-Δ9 unsaturated triacylglycerols. Thus, using different cultivation conditions, the production of recombinant lipase B was optimised, yielding 200 000 Units per liter culture. After overexpression lipase B was purified by diafiltration (372 U/mg). The investigated enzyme properties were comparable to those reported for the native enzyme.

AB - Lipase A and B from Geotrichum candidum CMICC 335426 were functionally expressed and secreted in Pichia pastoris. Lipase B exhibits a unique substrate specificity for long-chain cis-Δ9 unsaturated triacylglycerols. Thus, using different cultivation conditions, the production of recombinant lipase B was optimised, yielding 200 000 Units per liter culture. After overexpression lipase B was purified by diafiltration (372 U/mg). The investigated enzyme properties were comparable to those reported for the native enzyme.

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Overexpression of lipase A and B of Geotrichum candidum in Pichia pastoris: High-level production and some properties of functional expressed lipase B

Abstract

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