María-Isabel González-Siso

Prof. María-Isabel González-Siso

Grupo EXPRELA, Centro de Investigacións Científicas Avanzadas (CICA), Departamento de Bioloxía Celular e Molecular, Facultade de Ciencias, Universidade da Coruña, Campus de A Coruña, 15071 A Coruña, Spain
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Research Focus & Metrics

Academic Career Length

40Years (1987-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 July 1996 in Bioresource Technology
Verified
Journal Article
Closed access
María-Isabel González-SisoMaría-Isabel González-Siso
María-Isabel González-Siso

31 May 2014 in Current Protein & Peptide Science
Verified
Journal Article
Open access
PDF file
OLOlalla Lopez-Lopez
Olalla Lopez-Lopez
M. Esperanza CerdánM. Esperanza Cerdán
M. Esperanza Cerdán
María-Isabel González-SisoMaría-Isabel González-Siso
María-Isabel González-Siso
Lipolytic enzymes catalyze the hydrolysis of ester bonds in the presence of water. In media with low water content or in organic solvents, they can catalyze synthetic reactions such as esterification and transesterification. Lipases and esterases, in particular those from extremophilic origin, are robust enzymes, functional under the harsh conditions of industrial processes owing to their inherent thermostability and resistance towards organic solvents, which combined with their high chemo-, regio- and enantioselectivity make them very attractive biocatalysts for a variety of industrial applications. Likewise, enzymes from extremophile sources can provide additional features such as activity at extreme temperatures, extreme pH values or high salinity levels, which could be interesting for certain purposes. New lipases and esterases have traditionally been discovered by the isolation of microbial strains producing lipolytic activity. The Genome Projects Era allowed genome mining, exploiting homology with known lipases and esterases, to be used in the search for new enzymes. The Metagenomic Era meant a step forward in this field with the study of the metagenome, the pool of genomes in an environmental microbial community. Current molecular biology techniques make it possible to construct total environmental DNA libraries, including the genomes of unculturable organisms, opening a new window to a vast field of unknown enzymes with new and unique properties. Here, we review the latest advances and findings from research into new extremophilic lipases and esterases, using metagenomic approaches, and their potential industrial and biotechnological applications.

1 April 2003 in Biochemical Pharmacology
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Journal Article
Closed access
JLJosé M. Leiro-Vidal
José M. Leiro-Vidal
Ezequiel AlvarezEzequiel Alvarez
Ezequiel Alvarez
JAJuan Alberto Arranz
Juan Alberto Arranz
María-Isabel González-SisoMaría-Isabel González-Siso
María-Isabel González-Siso
FOFrancisco Orallo
Francisco Orallo

27 September 2016 in Frontiers in Microbiology
Verified
Journal Article
Open access
MDMaría-Eugenia DeCastro
María-Eugenia DeCastro
M. Esther Rodríguez-BelmonteM. Esther Rodríguez-Belmonte
M. Esther Rodríguez-Belmonte
María-Isabel González-SisoMaría-Isabel González-Siso
María-Isabel González-Siso
Microbial populations living in environments with temperatures above 50ºC (thermophiles) have been widely studied, increasing our knowledge in the composition and function of these ecological communities. Since these populations express a broad number of heat-resistant enzymes (thermozymes), they also represent an important source for novel biocatalysts that can be potentially used in industrial processes. The integrated study of the whole-community DNA from an environment, known as metagenomics, coupled with the development of next generation sequencing (NGS) technologies, has allowed the generation of large amounts of data from thermophiles. In this review, we summarize the main approaches commonly utilized for assessing the taxonomic and functional diversity of thermophiles through metagenomics, including several bioinformatics tools and some metagenome-derived methods to isolate their thermozymes.

1 February 2012 in Journal of Structural Biology
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Journal Article
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ÁPÁngel Pereira-Rodríguez
Ángel Pereira-Rodríguez
RFRafael Fernández-Leiro
Rafael Fernández-Leiro
María-Isabel González-SisoMaría-Isabel González-Siso
María-Isabel González-Siso
M. Esperanza CerdánM. Esperanza Cerdán
M. Esperanza Cerdán
Manuel BecerraManuel Becerra
Manuel Becerra
JSJulia Sanz-Aparicio
Julia Sanz-Aparicio

25 April 2013 in Life
Verified
Journal Article
Open access
PDF file
OLOlalla López-López
Olalla López-López
M. Esperanza CerdánM. Esperanza Cerdán
M. Esperanza Cerdán
María-Isabel González-SisoMaría-Isabel González-Siso
María-Isabel González-Siso
Hot springs have been investigated since the XIX century, but isolation and examination of their thermophilic microbial inhabitants did not start until the 1950s. Many thermophilic microorganisms and their viruses have since been discovered, although the real complexity of thermal communities was envisaged when research based on PCR amplification of the 16S rRNA genes arose. Thereafter, the possibility of cloning and sequencing the total environmental DNA, defined as metagenome, and the study of the genes rescued in the metagenomic libraries and assemblies made it possible to gain a more comprehensive understanding of microbial communities—their diversity, structure, the interactions existing between their components, and the factors shaping the nature of these communities. In the last decade, hot springs have been a source of thermophilic enzymes of industrial interest, encouraging further study of the poorly understood diversity of microbial life in these habitats.