Paper Report for: Costa_2009_Bioprocess.Biosyst.Eng_32_53
Reference
Title: Enhancing the thermal stability of lipases through mutagenesis and immobilization on zeolites Costa L, Brissos V, Lemos F, Ribeiro FR, Cabral JM Ref: Bioprocess Biosyst Eng, 32:53, 2009 : PubMed
The hydrolysis reaction of p-nitrophenyl butyrate catalyzed by lipases was followed with in situ UV/vis diode array spectrophotometry. Five enzymes - Candida antarctica lipase B and Fusarium solani pisi cutinase wild-type and three single-mutation variants - were tested as catalysts in homogeneous conditions and immobilized on zeolite NaY, on a polyacrylate support and as cross-linked aggregates. Using deconvolution techniques and kinetic modeling, the thermal stability of the different biocatalysts was compared in operational conditions and the results were supported by steady-state enzyme fluorescence measurements. We concluded that both the mutagenesis and the immobilization on zeolite NaY had a positive effect on the thermal stability of F. solani pisi cutinase.
        
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Costa L, Brissos V, Lemos F, Ribeiro FR, Cabral JM (2009) Enhancing the thermal stability of lipases through mutagenesis and immobilization on zeolites Bioprocess Biosyst Eng32: 53-61
Costa L, Brissos V, Lemos F, Ribeiro FR, Cabral JM (2009) Bioprocess Biosyst Eng32: 53-61