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ON THE INTERFACIAL ACTIVATION OF CANDIDA-ANTARCTICA LIPASE-A AND LIPASE-B AS COMPARED WITH HUMICOLA-LANUGINOSA LIPASE
KTH, Skolan för bioteknologi (BIO), Biokemi (stängd 20130101).ORCID-id: 0000-0002-2993-9375
1995 (engelsk)Inngår i: BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM, ISSN 0005-2760, Vol. 1258, nr 3, s. 272-276Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The interfacial activation of Candida antarctica lipase A (CALA) and B (CALB) has been investigated and compared with that of Humicola lanuginosa lipase (HLL). CALB displayed no interfacial activation towards p-nitrophenyl butyrate (PNPB) when exceeding the solubility limit of the substrate. No activation was observed towards p-nitrophenyl acetate (PNPA) at the addition of sodium dodecyl sulfate (SDS) nor in the presence of a solid polystyrene surface. The catalytic action of CALB was very different from that of Humicola lanuginosa lipase, which showed a pronounced interfacial activation with the same substrates. The basis for the anomalous behaviour of CALB is proposed to be due to the absence of a lid that regulates the access to the active site. in contrast to CALB, CALA expressed interfacial activation, but the activation was not as prominent as for Humicola lanuginosa lipase (HLL). The structural basis for the activation of CALA is unknown.

sted, utgiver, år, opplag, sider
ROYAL INST TECHNOL,DEPT BIOCHEM & BIOTECHNOL,S-10044 STOCKHOLM,SWEDEN.: ELSEVIER SCIENCE BV , 1995. Vol. 1258, nr 3, s. 272-276
Emneord [en]
EMULSION, WATER SOLUBLE, P-NITROPHENYL ESTER, ADSORPTION, SODIUM DODECYL SULFATE
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Identifikatorer
URN: urn:nbn:se:kth:diva-225147DOI: 10.1016/0005-2760(95)00131-UISI: A1995RY99400008PubMedID: 7548197OAI: oai:DiVA.org:kth-225147DiVA, id: diva2:1194361
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QCR 20180405

Tilgjengelig fra: 2018-04-01 Laget: 2018-04-01 Sist oppdatert: 2018-04-05bibliografisk kontrollert

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