Synthesis of a green polyurethane foam from a biopolyol obtained by enzymatic glycerolysis and its use for immobilization of lipase NS-40116

The use of green sources for materials synthesis has gained popularity in recent years. This work investigated the immobilization of lipase NS-40116 ( Thermomyces lanuginosus lipase) in polyurethane foam (PUF) using a biopolyol obtained through the enzymatic glycerolysis between castor oil and glyce...

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Bibliographic Details
Published in:	Bioprocess and biosystems engineering Vol. 42; no. 2; pp. 213 - 222
Main Authors:	Bresolin, Daniela, Estrella, Arthur S., da Silva, Jacqueline R. P., Valério, Alexsandra, Sayer, Cláudia, de Araújo, Pedro H. H., de Oliveira, Débora
Format:	Journal Article
Language:	English
Published:	Berlin/Heidelberg Springer Berlin Heidelberg 01-02-2019 Springer Nature B.V
Subjects:	Biocatalysis Biotechnology Biotechnology - methods Bulk density Calcium Castor oil Chemistry Chemistry and Materials Science Conversion Diglycerides Environmental Engineering/Biotechnology Environmental Microbiology Enzymes, Immobilized - chemistry Esterification Esters Ethanol Fatty acid methyl esters Food Science Glycerol Glycerol - chemistry Green Chemistry Technology - methods High temperature Immobilization Industrial and Production Engineering Industrial Chemistry/Chemical Engineering Kinetics Lipase Lipase - chemistry Magnesium pH effects Polymers - chemistry Polyurethane Polyurethane foam Polyurethanes - chemical synthesis Polyurethanes - chemistry Propanol Research Paper Solvents Spectroscopy, Fourier Transform Infrared Synthesis Temperature Biopolyol Biocatalysis Lipase NS-40116 Environmental biotechnology Polyurethane foam Lipase immobilization
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Summary:	The use of green sources for materials synthesis has gained popularity in recent years. This work investigated the immobilization of lipase NS-40116 ( Thermomyces lanuginosus lipase) in polyurethane foam (PUF) using a biopolyol obtained through the enzymatic glycerolysis between castor oil and glycerol, catalyzed by the commercial lipase Novozym 435 for the PUF formation. The reaction was performed to obtain biopolyol resulting in the conversion of 64% in mono- and diacylglycerol, promoting the efficient use of the reaction product as biopolyol to obtain polyurethane foam. The enzymatic derivative with immobilized lipase NS-40116 presented apparent density of 0.19 ± 0.03 g/cm 3 and an immobilization yield was 94 ± 4%. Free and immobilized lipase NS-40116 were characterized in different solvents (methanol, ethanol, and propanol), temperatures (20, 40, 60 and 80 °C), pH (3, 5, 7, 9 and 11) and presence of ions Na + , Mg ++ , and Ca ++ . The support provided higher stability to the enzyme, mainly when subjected to acid pH (free lipase lost 80% of relative activity after 360 h of contact, when the enzymatic derivative lost around 22%) and high-temperature free lipase lost 50% of relative activity, while the immobilized remained 95%. The enzymatic derivative was also used for esterification reactions and conversions around 66% in fatty acid methyl esters, using abdominal chicken fat as feedstock, were obtained in the first use, maintaining this high conversion until the fourth reuse, proving that the support obtained using environmentally friendly techniques is applicable.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1615-7591 1615-7605
DOI:	10.1007/s00449-018-2026-9