Enzymatic production of biodiesel : Strategies to overcome methanol inactivation
Lotti, Marina (Università degli Studi Milano-Bicocca. Dipartimento di Biotecnologie e Bioscienze)
Pleiss, Jürgen (University of Stuttgart. Institute of Biochemistry and Technical Biochemistry)
Valero Barranco, Francisco (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Ferrer, Pau (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)

Date:	2018
Abstract:	Lipase-catalyzed transesterification of triglycerides and alcohols to obtain biodiesel is an environmentally friendly and sustainable route for fuels production since, besides proceeding in mild reaction conditions, it allows for the use of low-cost feedstocks that contain water and free fatty acids, for example non-edible oils and waste oils. This review article reports recent advances in the field and focus in particular on a major issue in the enzymatic process, the inactivation of most lipases caused by methanol, the preferred acyl acceptor used for alcoholysis. The recent results about immobilization of enzymes on nano-materials and the use of whole-cell biocatalysts, as well as the use of cell-surface display technologies and metabolic engineering strategies for microbial production of biodiesel are described. It is discussed also insight into the effects of methanol on lipases obtained by modeling approaches and report on studies aimed at mining novel alcohol stable enzymes or at improving robustness in existing ones by protein engineering.
Grants:	Ministerio de Economía y Competitividad CTQ2016-74959-R Agència de Gestió d'Ajuts Universitaris i de Recerca 2014/SGR-452
Rights:	Tots els drets reservats.
Language:	Anglès
Document:	Article ; recerca ; Versió acceptada per publicar
Subject:	Biodiesel ; Immobilization ; Lipase ; Methanol ; Sustainability
Published in:	Biotechnology Journal, Vol. 13, Issue 5 (May 2018) , art. 1700155, ISSN 1860-7314

DOI: 10.1002/biot.201700155
PMID: 29461685

Postprint 28 p, 460.0 KB

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