Manuel García Ferrer - Catalysis

Author Information

Manuel García Ferrer is affiliated with the Institute of Catalysis, Consejo Superior de Investigaciones Científicas (CSIC) in Madrid, Spain. His research focuses on various aspects of catalysis, including enzyme functionality, substrate promiscuity, and photocatalysts. His work often involves a combination of computational and experimental approaches to understand and enhance catalytic processes.

Research Contributions

In 2021, Manuel García Ferrer authored numerous significant publications, contributing to the understanding of enzyme mechanisms and catalytic processes. His research includes the discovery of novel bifunctional enzymes, computational design of enzyme promiscuity, and the use of metabolomics to study synergistic effects in photocatalysts. Additionally, he has explored the functionality of proteases, bile metagenomes, and bone-degrading enzymes, providing insights into their potential applications in industrial and environmental processes.

Aliases

M Ferrer, Manuel García Ferrer, Manuel Ferrer

Publication and Citation Metrics

Metric	Value
Total Citations	11,586
H-index	61
Number of Papers	249

Publications:

The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity

DOI: 10.1038/s41598-021-91536-1

Year: 2021

Computationally Driven Rational Design of Substrate Promiscuity on Serine Ester Hydrolases

DOI: 10.1021/ACSCATAL.0C05015

Year: 2021

Structure and evolutionary trace-assisted screening of a residue swapping the substrate ambiguity and chiral specificity in an esterase

DOI: 10.1016/j.csbj.2021.04.041

Year: 2021

Metabolomics reveals synergy between Ag and g-C3N4 in Ag/g-C3N4 composite photocatalysts: a unique feature among Ag-doped biocidal materials.

DOI: 10.1007/s11306-021-01804-4

Year: 2021

Two-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range

DOI: 10.1007/s00253-021-11235-9

Year: 2021

Functional Characterisation of Bile Metagenome: Study of Metagenomic Dark Matter

DOI: 10.3390/microorganisms9112201

Year: 2021

The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity

DOI: 10.21203/RS.3.RS-269983/V1

Year: 2021

ω-Transaminase-Mediated Asymmetric Synthesis of (S)-1-(4-Trifluoromethylphenyl)Ethylamine

DOI: 10.3390/CATAL11030307

Year: 2021

The bone-degrading enzyme machinery: From multi-component understanding to the treatment of residues from the meat industry

DOI: 10.1016/j.csbj.2021.11.027

Year: 2021

Deciphering a Marine Bone-Degrading Microbiome Reveals a Complex Community Effort

DOI: 10.1128/mSystems.01218-20

Year: 2021

How Are Catalysts Prepared for Experimental Trials?

How are Inter Laboratory Comparisons Conducted?

How does HREM contribute to catalysis research?

What Are Self-Cleaning Filters?

How to Troubleshoot Common Issues?

What Happens When Surface Area Decreases?

Why Are Records Important?

What is Thermodynamic Data in Catalysis?

What Types of Predictive Models Are Used?

What Resources Are Available Post-Workshop?

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