Applied Biochemistry and Biotechnology

, Volume 189, Issue 3, pp 903–918 | Cite as

Screening and Immobilization of Interfacial Esterases from Marine Invertebrates as Promising Biocatalyst Derivatives

  • Alberto del Monte-MartínezEmail author
  • Jorge González-Bacerio
  • Carlos M. Varela
  • Fernando Vega-Villasante
  • Rogelio Lalana-Rueda
  • Héctor Nolasco
  • Joaquín Díaz
  • José M. Guisán


Interfacial esterases are useful enzymes in bioconversion and racemic mixture resolution processes. Marine invertebrates are few explored potential sources of these proteins. In this work, aqueous extracts of 41 species of marine invertebrates were screened for esterase, lipase, and phospholipase A activities, being all positive. Five extracts (Stichodactyla helianthus, Condylactis gigantea, Stylocheilus longicauda, Zoanthus pulchellus, and Plexaura homomalla) were selected for their activity values and immobilized on Octyl-Sepharose CL 4B support by interfacial adsorption. The selectivity of this immobilization method for interfacial esterases was evidenced by immobilization percentages ≥ 94% in almost all cases for lipase and phospholipase A activities. Six pharmaceutical-relevant esters (phenylethyl butyrate, ethyl-2-hydroxy-4-phenyl-butanoate, 2-oxyranylmethyl acetate (glycidol acetate), 7-aminocephalosporanic acid, methyl-prostaglandin F, and methyl-6-metoxy-α-methyl-2-naphtalen-acetate -naproxen methyl ester-) were bioconverted by at least three of these biocatalysts, with the lowest conversion percentage of 24%. In addition, three biocatalysts were used in the racemic mixture resolution of three previous compounds. The S. helianthus–derived biocatalyst showed the highest enantiomeric ratios for glycidol acetate (2.67, (S)-selective) and naproxen methyl ester (8.32, (R)-selective), and the immobilized extract of S. longicauda was the most resolutive toward the ethyl-2-hydroxy-4-phenyl-butanoate (8.13, (S)-selective). These results indicate the relevance of such marine interfacial esterases as immobilized biocatalysts for the pharmaceutical industry.


Enzymatic bioconversion Interfacial adsorption Interfacial esterases Marine invertebrates Pharmaceutical-relevant esters Racemic mixture resolution 



We are grateful to ICP-CSIC, Madrid, Spain, and CQF-MINSAP, La Habana, Cuba, for supplying several model compounds used in this analysis.

Funding Information

The authors wish to thank INFORMATICA ddmm., Bergamo, Italy, for kindly providing financial support to A. del Monte. Thanks to Havana University, Cuba; ICP-CSIC, Madrid, Spain and CONACyT, México for scientific grants.

Compliance with Ethical Standards

Conflict of Interest

The authors declare that they have no conflict of interest.


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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Alberto del Monte-Martínez
    • 1
    Email author
  • Jorge González-Bacerio
    • 1
    • 2
  • Carlos M. Varela
    • 3
    • 4
  • Fernando Vega-Villasante
    • 5
  • Rogelio Lalana-Rueda
    • 6
  • Héctor Nolasco
    • 7
  • Joaquín Díaz
    • 1
  • José M. Guisán
    • 8
  1. 1.Centro de Estudio de Proteínas, Facultad de BiologíaUniversidad de La HabanaHavanaCuba
  2. 2.Departamento de Bioquímica, Facultad de BiologíaUniversidad de La HabanaHavanaCuba
  3. 3.Rosenstiel School of Marine and Atmospheric Science (RSMAS)University of MiamiMiamiUSA
  4. 4.Florida International UniversityMiamiUSA
  5. 5.Centro Universitario de La CostaUniversidad de GuadalajaraPuerto VallartaMexico
  6. 6.Centro de Investigaciones MarinasUniversidad de La HabanaHavanaCuba
  7. 7.Centro de Investigaciones Biológicas del NoroesteConsejo Nacional de Ciencia y Tecnología (CONACyT)La PazMexico
  8. 8.Departamento de Biocatálisis, Instituto de Catálisis y PetroleoquímicaConsejo Superior de Investigaciones Científicas (CSIC) Campus CantoblancoMadridSpain

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