Alcohol oxidase from the yeast Pichia pastoris – a potential catalyst for organic synthesis

Dienys, Gervydas; Jarmalavičius, Saulius; Budrienė, Saulutė; Čitavičius, Donaldas Jonas; Sereikaitė, Jolanta

doi:10.1016/S1381-1177(02)00135-2

Use this URL to cite this publication: https://hdl.handle.net/20.500.14911/132810

Alcohol oxidase from the yeast Pichia pastoris – a potential catalyst for organic synthesis

Details

Publication Type (CRIS)

Straipsnis Web of Science duomenų bazėje / Article in Web of Science database (S1a)

Publication Type (eLABa)

Straipsnis Web of Science DB / Web of Science DB article (S1)

Author(s)

Author	Affiliation
Dienys, Gervydas	Vilniaus universitetas
Jarmalavičius, Saulius	Biotechnologijos institutas
Budrienė, Saulutė	Vilniaus universitetas
Čitavičius, Donaldas Jonas	Vilniaus universitetas
Sereikaitė, Jolanta	Chemijos ir bioinžinerijos katedra / Department of Chemistry and Bioengineering (1032)

Title

Alcohol oxidase from the yeast Pichia pastoris – a potential catalyst for organic synthesis

[en]

Gervydas Dienys, Saulius Jarmalavičius, Saulutė Budrienė, Donaldas Jonas Čitavičius, Jolanta Sereikaitė

Is part of

Journal of molecular catalysis B : Enzymatic

Published In

Year	Volume	Issue	Start Page	End Page
2003	21	1-2	47	49

Publisher

Amsterdam : Elsevier

Publisher (trusted)

Elsevier

Referenced in Database(s)(DBs)

Chemical abstracts

Compendex

Science Citation Index Expanded (Web of Science)

Extent

p. 47-49

URI

URI	Access Rights
https://hdl.handle.net/20.500.14911/132810
Straipsnis	Viso teksto dokumentas (atviroji prieiga) / Full Text Document (Open Access)

DOI

10.1016/S1381-1177(02)00135-2

Cited references

Science / Art Area

Technologijos mokslai / Technological sciences (T)

Field of Science / Art

Chemijos inžinerija / Chemical engineering (T005)

Chemija / Chemistry (N003)

Biochemija / Biochemistry (N004)

Keywords (en)

Abstract (en)

Alcohol oxidase (AO) from the methylotropic yeast Pichia pastoris was isolated and investigated. Wide substrate specificity is characteristic for this enzyme. Unbranched primary alcohols are effectively oxidized by AO to aldehydes, including propargyl alcohol, 2-chloroethanol, 2-cyanoethanol, leading to important synthetic intermediates. AO was immobilized by covalent linking to macroporous cellulose activated by glutaraldehyde, yield of immobilization 80%. Presence of two izoenzymes of AO was suggested from the pH activity dependence.