Polyphenylacetylene (PPA) was studied and characterized as a new matrix for Candida rugosa lipase (CRL) immobilization, establishing pi interactions with the enzyme. Performances of the new biocatalytic system were compared to different hydrophobic matrices (cross-linked polyvinyl alcohol esterified with lauric acid-CL-PVA-C-12, commercial polypropylene-EP-100, commercial Sepabeads functionalized with C-18 chains, treated and untreated with polyethyleneimine-C-18-SEPA-PEI and C-18-SEPA). Hydrophobic interactions between carriers and enzyme are the main forces involved. The immobilized enzyme showed a higher stability to T and pH changes and to organic solvents as media than the free one. Moreover, for transesteritication reactions carried out in organic solvents, increased initial rate and enantioselectivity were observed for the immobilized enzyme compared to those of the free one. PPA, when compared to the other supports, showed a good performance in terms of activity and enantioselectivity suggesting a possible use as a new lipase carrier. (C) 2004 Elsevier B.V. All rights reserved.
Acetylenic polymers as new immobilization matrices for lipolytic enzymes / F., Panzavolta; S., Soro; R., D'Amato; Palocci, Cleofe; Cernia, Enrico; Russo, Maria Vittoria. - In: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC. - ISSN 1381-1177. - STAMPA. - 32:3(2005), pp. 67-76. [10.1016/j.molcatb.2004.09.011]
Acetylenic polymers as new immobilization matrices for lipolytic enzymes
PALOCCI, Cleofe;CERNIA, Enrico;RUSSO, Maria Vittoria
2005
Abstract
Polyphenylacetylene (PPA) was studied and characterized as a new matrix for Candida rugosa lipase (CRL) immobilization, establishing pi interactions with the enzyme. Performances of the new biocatalytic system were compared to different hydrophobic matrices (cross-linked polyvinyl alcohol esterified with lauric acid-CL-PVA-C-12, commercial polypropylene-EP-100, commercial Sepabeads functionalized with C-18 chains, treated and untreated with polyethyleneimine-C-18-SEPA-PEI and C-18-SEPA). Hydrophobic interactions between carriers and enzyme are the main forces involved. The immobilized enzyme showed a higher stability to T and pH changes and to organic solvents as media than the free one. Moreover, for transesteritication reactions carried out in organic solvents, increased initial rate and enantioselectivity were observed for the immobilized enzyme compared to those of the free one. PPA, when compared to the other supports, showed a good performance in terms of activity and enantioselectivity suggesting a possible use as a new lipase carrier. (C) 2004 Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
