What is he best known for?
The fields of study he is best known for:
- Enzyme
- Organic chemistry
- Biochemistry
Ángel T. Martínez spends much of his time researching Lignin, Organic chemistry, Laccase, Biochemistry and Pleurotus eryngii. The study incorporates disciplines such as Peroxidase, Lignin peroxidase, Manganese peroxidase, Pulp and Nuclear magnetic resonance spectroscopy in addition to Lignin. In Organic chemistry, Ángel T. Martínez works on issues like Two-dimensional nuclear magnetic resonance spectroscopy, which are connected to Acylation and Pectin.
The Laccase study combines topics in areas such as Cellulose, Botany and Pulp and paper industry. Ángel T. Martínez interconnects Food science and Mycelium in the investigation of issues within Biochemistry. His study in the field of Aryl-alcohol oxidase also crosses realms of Pleurotus ostreatus.
His most cited work include:
- The paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes (1059 citations)
- Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin (829 citations)
- Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion (490 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of study are Lignin, Biochemistry, Organic chemistry, Laccase and Peroxidase. As a member of one scientific family, Ángel T. Martínez mostly works in the field of Lignin, focusing on Straw and, on occasion, Food science. Biochemistry is often connected to Pleurotus eryngii in his work.
His study in the field of Pycnoporus cinnabarinus is also linked to topics like ABTS. In his study, which falls under the umbrella issue of Peroxidase, Oxidoreductase is strongly linked to Stereochemistry. His work carried out in the field of Pulp brings together such families of science as Kraft paper and Eucalyptus globulus.
He most often published in these fields:
- Lignin (40.60%)
- Biochemistry (25.46%)
- Organic chemistry (24.08%)
What were the highlights of his more recent work (between 2014-2021)?
- Lignin (40.60%)
- Peroxidase (19.72%)
- Stereochemistry (10.32%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Lignin, Peroxidase, Stereochemistry, Enzyme and Biochemistry. His study in Lignin is interdisciplinary in nature, drawing from both Directed mutagenesis, Laccase and Pulp and paper industry. His research in Peroxidase intersects with topics in Tryptophan and Electron transfer.
His Enzyme study combines topics from a wide range of disciplines, such as Hydrogen peroxide and Escherichia coli. His Biochemistry research integrates issues from Depolymerization and Computational biology. His Versatile peroxidase study combines topics in areas such as Lignosulfonates and Pleurotus eryngii.
Between 2014 and 2021, his most popular works were:
- Differences in the chemical structure of the lignins from sugarcane bagasse and straw. (123 citations)
- Oxidoreductases on their way to industrial biotransformations (106 citations)
- 5-hydroxymethylfurfural conversion by fungal aryl-alcohol oxidase and unspecific peroxygenase. (87 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Organic chemistry
- Biochemistry
The scientist’s investigation covers issues in Lignin, Organic chemistry, Biochemistry, Peroxidase and Laccase. His Lignin research is multidisciplinary, incorporating elements of Ether, Versatile peroxidase and Straw. Many of his research projects under Organic chemistry are closely connected to Tricin with Tricin, tying the diverse disciplines of science together.
His Biochemistry research includes elements of Depolymerization and Pleurotus eryngii. His Peroxidase research is multidisciplinary, incorporating perspectives in Heme, Polyporales, Enzyme kinetics and Stereochemistry. His work deals with themes such as Rational design, Aniline, Directed evolution, Electron transfer and Enzymatic hydrolysis, which intersect with Laccase.
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