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Lipases and Phospholipases
Methods and Protocols

Edited by

Georgina Sandoval
Industrial Biotechnology Unit, Centro de Investigación y Asistencia en Tecnología y Diseño
del Estado de Jalisco A.C. (CIATEJ), Guadalajara, Jalisco, Mexico
Editor
Georgina Sandoval, Ph.D.
Industrial Biotechnology Unit
Centro de Investigación y Asistencia
en Tecnología y Diseño del Estado
de Jalisco A.C. (CIATEJ)
Guadalajara, Jalisco, Mexico

ISSN 1064-3745 ISSN 1940-6029 (electronic)

ISBN 978-1-61779-599-2 ISBN 978-1-61779-600-5 (eBook)
DOI 10.1007/978-1-61779-600-5
Springer New York Heidelberg Dordrecht London

Library of Congress Control Number: 2012933441

© Springer Science+Business Media New York 2012

This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is
concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction
on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation,
computer software, or by similar or dissimilar methodology now known or hereafter developed. Exempted from this
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Duplication of this publication or parts thereof is permitted only under the provisions of the Copyright Law of the
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The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not
imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws
and regulations and therefore free for general use.
While the advice and information in this book are believed to be true and accurate at the date of publication, neither
the authors nor the editors nor the publisher can accept any legal responsibility for any errors or omissions that may
be made. The publisher makes no warranty, express or implied, with respect to the material contained herein.

Printed on acid-free paper

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Springer is part of Springer Science+Business Media (www.springer.com)
Preface

Lipases are nowadays the most applied enzymes in organic synthesis because of their broad
substrate acceptance and because of the availability of the molecular, biochemical, thermo-
dynamical, and solvent engineering tools, which allows the optimization of lipases and
lipase-catalyzed reactions. We compile in this volume the arsenal of those tools and meth-
ods to succeed in your screening, optimization, and application of lipases.
On the other hand, phospholipases are emerging as useful enzymes in food and phar-
maceutical industries. As examples, their relationships with eicosanoids and protein kinases
(and therefore their related diseases) are well known, and the quest of food-grade phospho-
lipases is a current need of the food industry. This volume will guide you through the
potential applications of phospholipases and their related methods.
Although many publications on both enzymes can be found in the research literature,
this volume provides an update of fundamental issues, current and new applications as well
as practical step-by-step protocols that were lacking, given the extensive applications of
lipases and the potential application of phospholipases and its inhibitors.
The chapters contained within this volume were contributed either by recognized
experts in the field or by promising young scientists, who kindly collaborated with their
invaluable know-how and expertise. Chapters are well explained and written at an accessible
level, so they can be easily read by both graduate students and skilled scientists.
The introductory chapters provide the overview on lipases and phospholipases, but also
on an old debate: the definition of the lipase/esterase concepts, proposing a new bio-
physico-chemical classification.
The introduction section is followed by practical screening protocols to discover/target
new or improved lipases, phospholipases, and its inhibitors (which are especially relevant for
the study and treatment of metabolic and inflammatory diseases). A reemerging source of
these enzymes–the plants–is also discussed.
In subsequent chapters, a review on heterologous expression systems for lipases is
presented as a prelude of examples and study cases on cloning, production, purification,
and characterization of selected lipases and phospholipases. Protocols covering diverse
organisms are presented: human, chicken, Steptomyces, Rhizopus, Staphylococcus, and an
extremophile thermophile bacterium (Thermus).
Commonly, limiting steps for industrial application of enzymes are the optimization of
activity, selectivity, and stability of the biocatalyst. Besides, the particular reaction and
operation conditions are indispensable. Therefore, the fourth part of the book presents
methods and tools to optimize lipases and phospholipase by molecular evolution, molecu-
lar modeling and rational immobilization, in addition to thermodynamic tools to optimize
reaction an operation conditions.
Finally, eight applications of lipases and phospholipases are presented. Either in tradi-
tional applications (food and lipids modifications), recently established applications (organic
synthesis), or in new (biodiesel, biopolymers, and biosensors) emerging fields.

v
vi Preface

I would like to express my gratitude to all colleagues and Springer–Humana Press staff
who contributed to the achievement of this book; starting with John Walker, the editor of
this series, who besides to give us the opportunity to be part of this exciting project, was
always helpful and supporting along the editing process. I also acknowledge the very
efficient technical help from David Casey and the kind and considerate fund of some color
figures by Patrick J. Marton, Senior Editor of Springer Protocols.
I am truly grateful to all authors by its outstanding collaboration. It was a pleasure
working with this team. Particular thanks to the members of the ENZNUT network from
the Ibero-American program for Science, Technology and Development (CYTED), who
participated in seven chapters.
It is my hope that this volume will become the preferred reference book for the large
scientific community working with lipases, phospholipases, and related enzymes.

Guadalajara, Mexico Georgina Sandoval, Ph.D.

Contents

Preface. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . v
Contributors. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . xi

PART I OVERVIEW OF LIPASES, PHOSPHOLIPASES AND RELATED ENZYMES

1 Lipases: An Overview . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 3
Leticia Casas-Godoy, Sophie Duquesne, Florence Bordes,
Georgina Sandoval, and Alain Marty
2 Lipases or Esterases: Does It Really Matter? Toward a New
Bio-Physico-Chemical Classification . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 31
Yassine Ben Ali, Robert Verger, and Abdelkarim Abousalham
3 Study of New Feruloyl Esterases to Understand Lipase Evolution:
The Case of Bacillus flexus. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 53
Mónica Sánchez-González, Allan Blanco-Gámez,
Roberto Parra-Saldívar, Juan Carlos Mateos-Díaz,
and María Isabel Estrada-Alvarado
4 Phospholipases: An Overview . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 63
Ahmed Aloulou, Yassine Ben Ali, Sofiane Bezzine,
Youssef Gargouri, and Michael H. Gelb

PART II SCREENING AND SOURCES OF LIPASES, PHOSPHOLIPASES

AND ITS INHIBITORS

5 High-Throughput Screening Method for Lipases/Esterases . . . . . . . . . . . . . . 89

Eduardo Mateos-Díaz, Jorge Alberto Rodríguez,
María de los Ángeles Camacho-Ruiz,
and Juan Carlos Mateos-Díaz
6 Functional-Based Screening Methods for Lipases, Esterases,
and Phospholipases in Metagenomic Libraries . . . . . . . . . . . . . . . . . . . . . . . . . 101
Dolores Reyes-Duarte, Manuel Ferrer,
and Humberto García-Arellano
7 Plant Lipases: Partial Purification of Carica papaya Lipase . . . . . . . . . . . . . . . . 115
Ivanna Rivera, Juan Carlos Mateos-Díaz,
and Georgina Sandoval
8 Plant Phospholipases: An Overview . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 123
Geliang Wang, Stephen Ryu, and Xuemin Wang
9 Lipase and Phospholipase Inhibitors: Design and Applications. . . . . . . . . . . . . 139
Mark E. Venable

vii
viii Contents

10 High-Throughput Assay of Secreted Phospholipases A2 Inhibitors. . . . . . . . . . 149

Wallace Thompson, Rob C. Oslund, James Bollinger,
Heather Ewing, and Michael H. Gelb

PART III CLONING, PRODUCTION, PURIFICATION AND CHARACTERIZATION

OFLIPASES AND PHOSPHOLIPASES

11 Heterologous Expression Systems for Lipases: A Review . . . . . . . . . . . . . . . . . 161

Francisco Valero
12 Streptomyces Phospholipase D Cloning and Production . . . . . . . . . . . . . . . . . . 179
Yozo Nakazawa
13 Cloning of PLD2 from Baculovirus for Studies
in Inflammatory Responses . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 201
Julian Gomez-Cambronero and Karen M. Henkels
14 Lipases Production by Solid-State Fermentation:
The Case of Rhizopus homothallicus in Perlite . . . . . . . . . . . . . . . . . . . . . . . . . 227
Susana Velasco-Lozano, Tania Volke-Sepulveda,
and Ernesto Favela-Torres
15 Lipases and Esterases from Extremophiles: Overview and Case Example
of the Production and Purification of an Esterase from
Thermus thermophilus HB27 . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 239
Pablo Fuciños, Roberto González, Estrella Atanes,
Ana Belén Fernández Sestelo, Nelson Pérez-Guerra,
Lorenzo Pastrana, and María Luisa Rúa
16 Purification, Biochemical and Kinetic Properties of Recombinant
Staphylococcus aureus Lipase. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 267
Habib Horchani, Ahmed Fendri, Hanen Louati, Adel Sayari,
Youssef Gargouri, and Robert Verger
17 Phospholipase A2 Purification and Characterization: A Case Study . . . . . . . . . 283
Aida Karray, Youssef Gargouri, Robert Verger, and Sofiane Bezzine

PART IV OPTIMIZATION OF THE BIOCATALYST AND REACTION CONDITIONS

18 The Yeast Yarrowia lipolytica as a Generic Tool for Molecular

Evolution of Enzymes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 301
Sophie Duquesne, Florence Bordes, Franck Fudalej,
Jean-Marc Nicaud, and Alain Marty
19 Molecular Modeling of Lipase Binding to a Substrate–Water Interface. . . . . . . 313
Christian C. Gruber and Jürgen Pleiss
20 Different Strategies for Hyperactivation of Lipase Biocatalysts . . . . . . . . . . . . . 329
Jose M. Palomo and Jose M. Guisan
21 Rational Design of Immobilized Lipases and Phospholipases . . . . . . . . . . . . . . 343
Alberto del Monte-Martínez and Bessy V. Cutiño-Avila
 Contents ix

22 Thermodynamical Methods for the Optimization

of Lipase-Catalyzed Reactions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 383
Edmundo Castillo, Alejandro Torres-Gavilán,
Georgina Sandoval, and Alain Marty

PART V APPLICATIONS OF LIPASES AND PHOSPHOLIPASES

23 Lipases as Biocatalysts for the Synthesis of Structured Lipids . . . . . . . . . . . . . . 403

Ram Chandra Reddy Jala, Peng Hu, Tiankui Yang,
Yuanrong Jiang, Yan Zheng, and Xuebing Xu
24 Lipase-Catalyzed Modification of Phenolic Antioxidants . . . . . . . . . . . . . . . . . 435
Pamela Torres, Dolores Reyes-Duarte, Antonio Ballesteros,
and Francisco J. Plou
25 Lipases as Catalysts in Synthesis of Fine Chemicals. . . . . . . . . . . . . . . . . . . . . . 445
Alicia Baldessari
26 Lipases in Green Chemistry: Acylation and Alcoholysis
on Steroids and Nucleosides . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 457
Alicia Baldessari and Luis E. Iglesias
27 Lipases as Biocatalyst for Biodiesel Production . . . . . . . . . . . . . . . . . . . . . . . . 471
Xiaohu Fan, Xochitl Niehus, and Georgina Sandoval
28 Synthesis of Biodegradable Polymers Using Biocatalysis
with Yarrowia lipolytica Lipase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 485
Karla A. Barrera-Rivera, Arturo Flores-Carreón,
and Antonio Martínez-Richa
29 Phospholipases in Food Industry: A Review . . . . . . . . . . . . . . . . . . . . . . . . . . 495
Víctor Casado, Diana Martín, Carlos Torres,
and Guillermo Reglero
30 Lipase and Phospholipase Biosensors: A Review . . . . . . . . . . . . . . . . . . . . . . . 525
Enrique J. Herrera-López

Index . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 545
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Contributors

ABDELKARIM ABOUSALHAM • Organization and Dynamics of Biological Membranes,

UMR 5246 ICBMS, CNRS-Université Claude Bernard Lyon 1,
Villeurbanne Cedex, France; Enzymology at interfaces and physiology of lipolysis,
UPR 9025, CNRS-Aix-Marseille Université, Marseille, France
AHMED ALOULOU • National School of Engineers of Sfax, University of Sfax,
Sfax, Tunisia
YASSINE BEN ALI • Laboratoire de Biochimie et de Génie Enzymatique des Lipases,
ENIS, University of Sfax, Sfax, Tunisia
ESTRELLA ATANES • Department of Food and Analytical Chemistry, University of Vigo,
Ourense, Spain
ALICIA BALDESSARI • Laboratorio de Biocatálisis, Departamento de Química
Orgánica y UMYMFOR, Facultad de Ciencias Exactas y Naturales,
Universidad de Buenos Aires, Buenos Aires, Argentina
ANTONIO BALLESTEROS • Departamento de Biocatálisis, Instituto de Catálisis
y Petroleoquímica, CSIC, Madrid, Spain
KARLA A. BARRERA-RIVERA • División de Ciencias Naturales y Exactas,
Departamento de Química, Universidad de Guanajuato, Guanajuato, Mexico
SOFIANE BEZZINE • National School of Engineers of Sfax, University of Sfax,
Sfax, Tunisia; Laboratoire de Biochimie et de Génie Enzymatique des Lipases,
Ecole Nationale d’Ingénieurs de Sfax, Sfax, Tunisia
ALLAN BLANCO-GÁMEZ • Universidad Autónoma de Nuevo León,
Facultad de Ciencias Químicas, Monterrey, Nuevo Leon, Mexico
JAMES BOLLINGER • Departments of Chemistry and Biochemistry, University
of Washington, Seattle, WA, USA
FLORENCE BORDES • Equipe de Catalyse et Ingénierie Moléculaire Enzymatique,
Laboratoire d’Ingénierie des Systèmes Biologiques et Procédés,
Université de Toulouse, INSA, UPS, INP, LISBP, Toulouse, France;
CNRS, UMR5504, Toulouse, France; INRA, UMR792, Ingénierie des
Systèmes Biologiques et des Procédés, Toulouse, France
MARÍA DE LOS ÁNGELES CAMACHO-RUIZ • Industrial Biotechnology Unit,
Centro de Investigación y Asistencia en Tecnología y Diseño del Estado
de Jalisco A.C. (CIATEJ), Guadalajara, Jalisco, Mexico
VÍCTOR CASADO • Departamento de Producción y Caracterización de Nuevos Alimentos,
Instituto de Investigación en Ciencias de la Alimentación (CIAL) (CSIC–UAM),
Madrid, Spain
LETICIA CASAS-GODOY • Equipe de Catalyse et Ingénierie Moléculaire Enzymatique,
Laboratoire d’Ingénierie des Systèmes Biologiques et Procédés, Université de
Toulouse, INSA, UPS, INP, LISBP, Toulouse, France; CNRS, UMR5504,
Toulouse, France; INRA, UMR792, Ingénierie des Systèmes Biologiques et des
Procédés, Toulouse, France

xi
xii Contributors

EDMUNDO CASTILLO • Instituto de Biotecnología, Universidad Nacional Autónoma

de México, Cuernavaca, Morelos, Mexico
BESSY V. CUTIÑO-AVILA • Facultad de Biología, Centro de Estudio de Proteínas,
Universidad de La Habana, La Habana, Cuba
SOPHIE DUQUESNE • Equipe de Catalyse et Ingénierie Moléculaire Enzymatique,
Laboratoire d’Ingénierie des Systèmes Biologiques et Procédés, Université de Toulouse,
INSA, UPS, INP, LISBP, Toulouse, France; CNRS, UMR5504, Toulouse, France;
INRA, UMR792, Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France
MARÍA ISABEL ESTRADA-ALVARADO • Instituto Tecnológico de Sonora (ITSON),
Sonora, Mexico
HEATHER EWING • Departments of Chemistry and Biochemistry, University
of Washington, Seattle, WA, USA
XIAOHU FAN • Piedmont Biofuels Industrial, Pittsboro, NC, USA
ERNESTO FAVELA-TORRES • Departamento de Biotecnología, Universidad Autónoma
Metropolitana-Iztapalapa, Mexico, Mexico
AHMED FENDRI • Laboratoire de Biochimie et de Génie Enzymatique des Lipases,
Ecole Nationale d’Ingénieurs de Sfax, Sfax, Tunisia
MANUEL FERRER • Departamento de Biocatálisis, Instituto de Catálisis
y Petroleoquímica, CSIC, Madrid, Spain
ARTURO FLORES-CARREÓN • División de Ciencias Naturales y Exactas,
Departamento de Biología, Universidad de Guanajuato, Guanajuato, Mexico
PABLO FUCIÑOS • Department of Food and Analytical Chemistry, University of Vigo,
Ourense, Spain
FRANCK FUDALEJ • Oxyrane Belgium NV, Gent-Zwijnaarde, Belgium
HUMBERTO GARCÍA-ARELLANO • Departamento de Procesos y Tecnología,
Universidad Autónoma Metropolitana, D.F. Mexico, Mexico
YOUSSEF GARGOURI • Laboratoire de Biochimie et de Génie Enzymatique des Lipases,
Ecole Nationale d’Ingénieurs de Sfax, Sfax, Tunisia
MICHAEL H. GELB • Departments of Chemistry and Biochemistry,
University of Washington, Seattle, WA, USA
JULIAN GOMEZ-CAMBRONERO • Department of Biochemistry and Molecular Biology,
Wright State University School of Medicine, Dayton, OH, USA
ROBERTO GONZÁLEZ • Department of Food and Analytical Chemistry,
University of Vigo, Ourense, Spain
CHRISTIAN C. GRUBER • ACIB Austrian Centre of Industrial Biotechnology,
c/o Centre of Molecular Biosciences, University of Graz, Graz, Austria
JOSE M. GUISAN • Departamento de Biocatálisis, Instituto de Catálisis
y Petroleoquímica, CSIC, Madrid, Spain
KAREN M. HENKELS • Department of Biochemistry and Molecular Biology,
Wright State University School of Medicine, Dayton, OH, USA
ENRIQUE J. HERRERA-LÓPEZ • Industrial Biotechnology Unit, Centro de Investigación
y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C. (CIATEJ),
Guadalajara, Jalisco, Mexico
HABIB HORCHANI • Laboratoire de Biochimie et de Génie Enzymatique des Lipases,
Ecole Nationale d’Ingénieurs de Sfax, Sfax, Tunisia
PENG HU • Wilmar Global R&D Center, Shanghai, China
 Contributors xiii

LUIS E. IGLESIAS • Laboratorio de Biotransformaciones, Departamento de Ciencia

y Tecnología, Universidad Nacional de Quilmes, Bernal, Buenos Aires, Argentina
RAM CHANDRA REDDY JALA • Wilmar Global R&D Center, Shanghai, China
YUANRONG JIANG • Wilmar Global R&D Center, Shanghai, China
AIDA KARRAY • Laboratoire de Biochimie et de Génie Enzymatique des Lipases,
Ecole Nationale d’Ingénieurs de Sfax, Sfax, Tunisia
HANEN LOUATI • Laboratoire de Biochimie et de Génie Enzymatique des Lipases,
Ecole Nationale d’Ingénieurs de Sfax, Sfax, Tunisia
DIANA MARTÍN • Departamento de Producción y Caracterización de Nuevos Alimentos,
Instituto de Investigación en Ciencias de la Alimentación (CIAL) (CSIC–UAM),
Madrid, Spain
ANTONIO MARTÍNEZ-RICHA • División de Ciencias Naturales y Exactas,
Departamento de Química, Universidad de Guanajuato, Guanajuato, Mexico
ALAIN MARTY • Equipe de Catalyse et Ingénierie Moléculaire Enzymatique,
Laboratoire d’Ingénierie des Systèmes Biologiques et Procédés, Université de Toulouse,
INSA, UPS, INP, LISBP, Toulouse, France; CNRS, UMR5504, Toulouse, France;
INRA, UMR792, Ingénierie des Systèmes Biologiques et des Procédés, Toulouse, France
EDUARDO MATEOS-DÍAZ • Industrial Biotechnology Unit, Centro de Investigación
y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C. (CIATEJ),
Guadalajara, Jalisco, Mexico
JUAN CARLOS MATEOS-DÍAZ • Industrial Biotechnology Unit, Centro de Investigación
y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C. (CIATEJ),
Guadalajara, Jalisco, Mexico
ALBERTO DEL MONTE-MARTÍNEZ • Centro de Estudio de Proteínas, Facultad de Biología,
Universidad de La Habana, La Habana, Cuba
YOZO NAKAZAWA • Department of Food and Cosmetic Science, Faculty of Bioindustry,
Tokyo University of Agriculture, Abashiri, Hokkaido, Japan
JEAN-MARC NICAUD • CNRS, MICALIS, Jouy-en-Josas, France
XOCHITL NIEHUS • Industrial Biotechnology Unit, Centro de Investigación
y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C. (CIATEJ),
Guadalajara, Jalisco, Mexico
ROB C. OSLUND • Departments of Chemistry and Biochemistry,
University of Washington, Seattle, WA, USA
JOSE M. PALOMO • Departamento de Biocatálisis, Instituto de Catálisis
y Petroleoquímica, CSIC, Madrid, Spain
ROBERTO PARRA-SALDÍVAR • Centro del agua para América Latina y el Caribe,
Instituto Tecnológico de Monterrey, Monterrey, Nuevo Leon, Mexico
LORENZO PASTRANA • Department of Food and Analytical Chemistry,
University of Vigo, Ourense, Spain
NELSON PÉREZ-GUERRA • Department of Food and Analytical Chemistry,
University of Vigo, Ourense, Spain
JÜRGEN PLEISS • Institute of Technical Biochemistry, University of Stuttgart,
Stuttgart, Germany
FRANCISCO J. PLOU • Departamento de Biocatálisis, Instituto de Catálisis
y Petroleoquímica, CSIC, Madrid, Spain
xiv Contributors

GUILLERMO REGLERO • Departamento de Producción y Caracterización de Nuevos

Alimentos, Instituto de Investigación en Ciencias de la Alimentación (CIAL)
(CSIC–UAM), Madrid, Spain
DOLORES REYES-DUARTE • Departamento de Procesos y Tecnología,
Universidad Autónoma Metropolitana, Unidad Cuajimalpa (UAM-C),
D.F. Mexico, Mexico
IVANNA RIVERA • Industrial Biotechnology Unit, Centro de Investigación
y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C. (CIATEJ),
Guadalajara, Jalisco, Mexico
JORGE ALBERTO RODRÍGUEZ • Industrial Biotechnology Unit, Centro de Investigación y
Asistencia en Tecnología y Diseño del Estado de Jalisco A.C. (CIATEJ),
Guadalajara, Jalisco, Mexico
MARÍA LUISA RÚA • Department of Food and Analytical Chemistry, University of Vigo,
Ourense, Spain
STEPHEN RYU • Korea Research Institute of Bioscience and Biotechnology, Yuseong-gu,
Daejeon, South Korea
MÓNICA SÁNCHEZ-GONZÁLEZ • Universidad Autónoma de Nuevo León,
Facultad de Ciencias Químicas, Monterrey, Nuevo Leon, Mexico
GEORGINA SANDOVAL • Industrial Biotechnology Unit, Centro de Investigación
y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C. (CIATEJ),
Guadalajara, Jalisco, Mexico
ADEL SAYARI • Laboratoire de Biochimie et de Génie Enzymatique des Lipases,
Ecole Nationale d’Ingénieurs de Sfax, Sfax, Tunisia
ANA BELÉN FERNÁNDEZ SESTELO • Department of Food and Analytical Chemistry,
University of Vigo, Ourense, Spain
WALLACE THOMPSON • Departments of Chemistry and Biochemistry,
University of Washington, Seattle, WA, USA
CARLOS TORRES • Departamento de Producción y Caracterización de Nuevos
Alimentos, Instituto de Investigación en Ciencias de la Alimentación (CIAL)
(CSIC–UAM), Madrid, Spain
PAMELA TORRES • Departamento de Biocatálisis, Instituto de Catálisis
y Petroleoquímica, CSIC, Madrid, Spain
ALEJANDRO TORRES-GAVILÁN • Instituto de Biotecnología, Universidad Nacional
Autónoma de México, Cuernavaca, Morelos, Mexico
FRANCISCO VALERO • Departament d’Enginyeria Química, EE. Universitat Autònoma
de Barcelona, Bellaterra, Barcelona, Spain
SUSANA VELASCO-LOZANO • Departamento de Biotecnología, Universidad Autónoma
Metropolitana-Iztapalapa, D.F. Mexico, Mexico
MARK E. VENABLE • Department of Biology, Appalachian State University,
Boone, NC, USA
ROBERT VERGER • Enzymology at interfaces and physiology of lipolysis,
CNRS-Aix-Marseille Université, UPR 9025, Marseille Cedex 20, France
TANIA VOLKE-SEPULVEDA • Departamento de Biotecnología, Universidad Autónoma
Metropolitana-Iztapalapa, D.F. Mexico, Mexico
 Contributors xv

GELIANG WANG • Department of Biology, University of Missouri, St. Louis, MO, USA;
Donald Danforth Center Plant Science Center, St. Louis, MO, USA
XUEMIN WANG • Department of Biology, University of Missouri, St. Louis, MO, USA;
Donald Danforth Center Plant Science Center, St. Louis, MO, USA
XUEBING XU • Department of Molecular Biology, Aarhus University, Aarhus, Denmark
TIANKUI YANG • Wilmar Global R&D Center, Shanghai, China
YAN ZHENG • Wilmar Global R&D Center, Shanghai, China
 Chapter 1

Lipases: An Overview
Leticia Casas-Godoy, Sophie Duquesne, Florence Bordes,
Georgina Sandoval, and Alain Marty

Abstract
Lipases are ubiquitous enzymes, widespread in nature. They were first isolated from bacteria in the early
nineteenth century and the associated research continuously increased due to the particular characteristics
of these enzymes. This chapter reviews the main sources, structural properties, and industrial applications
of these highly studied enzymes.

Key words: Lipases, Structure, a/b Hydrolase fold, Lid, Oxyanion hole, Catalytic triad, Catalytic
mechanism, Selectivity, Applications

1. Definition
of Lipases
Lipases are serine hydrolases defined as triacylglycerol acylhydrolases
(E.C. 3.1.1.3) and should be differentiated from esterases (E.C.
3.1.1.1) by the nature of their substrates. Indeed, the first criteria
used to distinguish these two types of enzymes, i.e., activation by
the presence of an interface, also called “interfacial activation,” was
found unsuitable for the classification of such enzymes as some
lipases did not exhibit such phenomenon. Prominent cases of this
phenomenon are Lip4 from Candida rugosa (1) and Candida ant-
arctica B (2). Moreover, lipases and esterases consensus motifs
described by ProSite database (3) are very close. Therefore, lipases
were later defined as enzymes capable of hydrolyzing carboxyl esters
of long-chain acylglycerol (³10 carbon atoms), while esterases hydro-
lyze carboxyl esters of short-chain acylglycerol (£10 carbon atoms).
Nevertheless, as both enzymes show a broad substrate specificity,

Georgina Sandoval (ed.), Lipases and Phospholipases: Methods and Protocols, Methods in Molecular Biology, vol. 861,
DOI 10.1007/978-1-61779-600-5_1, © Springer Science+Business Media New York 2012

3
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