Immobilization of Moniliella spathulata R25L270 Lipase on Ionic, Hydrophobic and Covalent Supports: Functional Properties and Hydrolysis of Sardine Oil

The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R...

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Published in:	Molecules (Basel, Switzerland) Vol. 22; no. 10; p. 1508
Main Authors:	Souza, Lívia, Moreno-Perez, Sonia, Fernández Lorente, Gloria, Cipolatti, Eliane, De Oliveira, Débora, Resende, Rodrigo, Pessela, Benevides
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 25.09.2017 MDPI
Subjects:	Biocatalysts Enzyme Stability Enzymes Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Fatty acids Fatty Acids, Omega-3 - metabolism fish oil Fish Oils - metabolism Hydrolysis Hydrophobic and Hydrophilic Interactions immobilization lipase Lipase - chemistry Lipase - metabolism Moniliella spathulata omega-3 Omega-3 fatty acids Yeasts - enzymology immobilization omega-3 Moniliella spathulata fish oil lipase
ISSN:	1420-3049, 1420-3049
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Abstract	The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating cis-5,8,11,15,17-eicosapentaenoic acid from sardine oil. The enzyme can act in a wide range of temperatures (25–48 °C) and pH (6.5–8.4). The present study deals with the immobilization of M. spathulata R25L270 lipase on hydrophobic, covalent and ionic supports to select the most active biocatalyst capable to obtain omega-3 fatty acids (PUFA) from sardine oil. Nine immobilized agarose derivatives were prepared and biochemically characterized for thermostability, pH stability and catalytic properties (KM and Vmax). Ionic supports improved the enzyme–substrate affinity; however, it was not an effective strategy to increase the M. spathulata R25L270 lipase stability against pH and temperature. Covalent support resulted in a biocatalyst with decreased activity, but high thermostability. The enzyme was most stabilized when immobilized on hydrophobic supports, especially Octyl-Sepharose. Compared with the free enzyme, the half-life of the Octyl-Sepharose derivative at 60 °C increased 10-fold, and lipase stability under acidic conditions was achieved. The Octyl-Sepharose derivative was selected to obtain omega-3 fatty acids from sardine oil, and the maximal enzyme selectivity was achieved at pH 5.0.
AbstractList	The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating cis-5,8,11,15,17-eicosapentaenoic acid from sardine oil. The enzyme can act in a wide range of temperatures (25–48 °C) and pH (6.5–8.4). The present study deals with the immobilization of M. spathulata R25L270 lipase on hydrophobic, covalent and ionic supports to select the most active biocatalyst capable to obtain omega-3 fatty acids (PUFA) from sardine oil. Nine immobilized agarose derivatives were prepared and biochemically characterized for thermostability, pH stability and catalytic properties (KM and Vmax). Ionic supports improved the enzyme–substrate affinity; however, it was not an effective strategy to increase the M. spathulata R25L270 lipase stability against pH and temperature. Covalent support resulted in a biocatalyst with decreased activity, but high thermostability. The enzyme was most stabilized when immobilized on hydrophobic supports, especially Octyl-Sepharose. Compared with the free enzyme, the half-life of the Octyl-Sepharose derivative at 60 °C increased 10-fold, and lipase stability under acidic conditions was achieved. The Octyl-Sepharose derivative was selected to obtain omega-3 fatty acids from sardine oil, and the maximal enzyme selectivity was achieved at pH 5.0. The oleaginous yeast R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba ( ) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating -5,8,11,15,17-eicosapentaenoic acid from sardine oil. The enzyme can act in a wide range of temperatures (25-48 °C) and pH (6.5-8.4). The present study deals with the immobilization of R25L270 lipase on hydrophobic, covalent and ionic supports to select the most active biocatalyst capable to obtain omega-3 fatty acids (PUFA) from sardine oil. Nine immobilized agarose derivatives were prepared and biochemically characterized for thermostability, pH stability and catalytic properties (K and V ). Ionic supports improved the enzyme-substrate affinity; however, it was not an effective strategy to increase the R25L270 lipase stability against pH and temperature. Covalent support resulted in a biocatalyst with decreased activity, but high thermostability. The enzyme was most stabilized when immobilized on hydrophobic supports, especially Octyl-Sepharose. Compared with the free enzyme, the half-life of the Octyl-Sepharose derivative at 60 °C increased 10-fold, and lipase stability under acidic conditions was achieved. The Octyl-Sepharose derivative was selected to obtain omega-3 fatty acids from sardine oil, and the maximal enzyme selectivity was achieved at pH 5.0. The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating cis-5,8,11,15,17-eicosapentaenoic acid from sardine oil. The enzyme can act in a wide range of temperatures (25-48 °C) and pH (6.5-8.4). The present study deals with the immobilization of M. spathulata R25L270 lipase on hydrophobic, covalent and ionic supports to select the most active biocatalyst capable to obtain omega-3 fatty acids (PUFA) from sardine oil. Nine immobilized agarose derivatives were prepared and biochemically characterized for thermostability, pH stability and catalytic properties (KM and Vmax). Ionic supports improved the enzyme-substrate affinity; however, it was not an effective strategy to increase the M. spathulata R25L270 lipase stability against pH and temperature. Covalent support resulted in a biocatalyst with decreased activity, but high thermostability. The enzyme was most stabilized when immobilized on hydrophobic supports, especially Octyl-Sepharose. Compared with the free enzyme, the half-life of the Octyl-Sepharose derivative at 60 °C increased 10-fold, and lipase stability under acidic conditions was achieved. The Octyl-Sepharose derivative was selected to obtain omega-3 fatty acids from sardine oil, and the maximal enzyme selectivity was achieved at pH 5.0.The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating cis-5,8,11,15,17-eicosapentaenoic acid from sardine oil. The enzyme can act in a wide range of temperatures (25-48 °C) and pH (6.5-8.4). The present study deals with the immobilization of M. spathulata R25L270 lipase on hydrophobic, covalent and ionic supports to select the most active biocatalyst capable to obtain omega-3 fatty acids (PUFA) from sardine oil. Nine immobilized agarose derivatives were prepared and biochemically characterized for thermostability, pH stability and catalytic properties (KM and Vmax). Ionic supports improved the enzyme-substrate affinity; however, it was not an effective strategy to increase the M. spathulata R25L270 lipase stability against pH and temperature. Covalent support resulted in a biocatalyst with decreased activity, but high thermostability. The enzyme was most stabilized when immobilized on hydrophobic supports, especially Octyl-Sepharose. Compared with the free enzyme, the half-life of the Octyl-Sepharose derivative at 60 °C increased 10-fold, and lipase stability under acidic conditions was achieved. The Octyl-Sepharose derivative was selected to obtain omega-3 fatty acids from sardine oil, and the maximal enzyme selectivity was achieved at pH 5.0.
Author	Resende, Rodrigo Souza, Lívia Pessela, Benevides Cipolatti, Eliane Fernández Lorente, Gloria De Oliveira, Débora Moreno-Perez, Sonia
AuthorAffiliation	6 Departamento de Engenharia e Tecnologías, Instituto Superior Politécnico de Tecnologías e Ciências (ISPTEC) Av. Luanda Sul, Rua Lateral Via S10, P.O. Box 1316, Talatona-Luanda Sul, Angola 3 Departamento de Biotecnología y Microbiología de Alimentos, Instituto de Investigación en Ciencias de la Alimentación CIAL (CSIC-UAM), Campus de la Universidad Autónoma de Madrid, Nicolás Cabrera 9, 28049 Madrid, Spain; gflorente@csic.es 2 Pharmacy and Biotechnology Department, School of Biomedical Sciences, Universidad Europea, Villaviciosa de Odón, 28670 Madrid, Spain; chaspy_27@hotmail.com 4 Departamento de Engenharia Química e Engenharia de Alimentos, Universidade Federal de Santa Catarina (UFSC), P.O. Box 476, Florianópolis SC 88040-900, Brazil; elianecipolatti@yahoo.com.br (E.P.C.); debora.oliveira@ufsc.br (D.d.O.) 5 Instituto Nanocell, Divinópolis MG 35500-041, Brazil 1 Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Avenida Presidente Antônio Carlos, 6627, Caixa P
AuthorAffiliation_xml	– name: 3 Departamento de Biotecnología y Microbiología de Alimentos, Instituto de Investigación en Ciencias de la Alimentación CIAL (CSIC-UAM), Campus de la Universidad Autónoma de Madrid, Nicolás Cabrera 9, 28049 Madrid, Spain; gflorente@csic.es – name: 1 Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Avenida Presidente Antônio Carlos, 6627, Caixa Postal 486, Belo Horizonte MG 31270-901, Brazil – name: 2 Pharmacy and Biotechnology Department, School of Biomedical Sciences, Universidad Europea, Villaviciosa de Odón, 28670 Madrid, Spain; chaspy_27@hotmail.com – name: 5 Instituto Nanocell, Divinópolis MG 35500-041, Brazil – name: 4 Departamento de Engenharia Química e Engenharia de Alimentos, Universidade Federal de Santa Catarina (UFSC), P.O. Box 476, Florianópolis SC 88040-900, Brazil; elianecipolatti@yahoo.com.br (E.P.C.); debora.oliveira@ufsc.br (D.d.O.) – name: 6 Departamento de Engenharia e Tecnologías, Instituto Superior Politécnico de Tecnologías e Ciências (ISPTEC) Av. Luanda Sul, Rua Lateral Via S10, P.O. Box 1316, Talatona-Luanda Sul, Angola
Author_xml	– sequence: 1 givenname: Lívia surname: Souza fullname: Souza, Lívia – sequence: 2 givenname: Sonia surname: Moreno-Perez fullname: Moreno-Perez, Sonia – sequence: 3 givenname: Gloria surname: Fernández Lorente fullname: Fernández Lorente, Gloria – sequence: 4 givenname: Eliane orcidid: 0000-0002-3272-712X surname: Cipolatti fullname: Cipolatti, Eliane – sequence: 5 givenname: Débora surname: De Oliveira fullname: De Oliveira, Débora – sequence: 6 givenname: Rodrigo surname: Resende fullname: Resende, Rodrigo – sequence: 7 givenname: Benevides surname: Pessela fullname: Pessela, Benevides
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Snippet	The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as... The oleaginous yeast R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba ( ) cake as substrate. The novel lipase was...
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SubjectTerms	Biocatalysts Enzyme Stability Enzymes Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Fatty acids Fatty Acids, Omega-3 - metabolism fish oil Fish Oils - metabolism Hydrolysis Hydrophobic and Hydrophilic Interactions immobilization lipase Lipase - chemistry Lipase - metabolism Moniliella spathulata omega-3 Omega-3 fatty acids Yeasts - enzymology
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Title	Immobilization of Moniliella spathulata R25L270 Lipase on Ionic, Hydrophobic and Covalent Supports: Functional Properties and Hydrolysis of Sardine Oil
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