Erick M. Peña-Lucio
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Erick M. Peña-Lucio has a total of 12 co-authors. Here are the top co-authors by number of shared publications:
- Abdulhameed Sabu
Kannur University
1 shared publication - Cristóbal N. Aguilar
Bioprocess and Bioproducts Research Group, Food Research Department, School of Chemistry, Autonomous University of Coahuila, Saltillo 25280, Mexico
1 shared publication - Emmanuel Flores-Hernández
Facultad de Ciencias Químicas, Universidad Autónoma de San Luis Potosí (UASLP), San Luis Potosí, México
1 shared publication - Fernando Luis Pieckenstain
Instituto Tecnológico de Chascomús (INTECH), Universidad Nacional de San Martín (UNSAM), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Chascomús, Argentina
1 shared publication - Hector Arturo Ruiz Leza
Biorefinery Group, Food Research Department, School of Chemistry, Universidad Autónoma de Coahuila, Saltillo 25280, Coahuila, Mexico
1 shared publication - José Luis Martínez Hernández
Bioprocesses and Bioproducts Research Group, Food Research Department, School of Chemistry, Universidad Autonoma de Coahuila, Saltillo 25280, Coahuila, Mexico
1 shared publication
Latest Publications
- 26 July 2025
- Published by Springer Nature in Physiology and Molecular Biology of Plants
- Vol. 31 (7) , 1053-1069
The polyamine uptake transporters PUT2/LAT4 and PUT5/LAT5 contribute to Arabidopsis defense response against Botrytis cinerea
Under biotic stress, plant polyamine metabolism undergoes significant changes, including increased biosynthesis and catabolism, which lead to hydrogen peroxide production. However, the roles of polyamine mobilization and transport across membranes remain elusive. Arabidopsis thaliana encodes five Polyamine Uptake Transporters (PUT1-PUT5). In this study, we investigated the role of polyamine transport in Arabidopsis during its interaction with the necrotrophic fungus Botrytis cinerea (Bc). Fungal inoculation induced the expression of all PUT/LAT genes at different times throughout disease progression. To assess their contribution to defense, we challenged five homozygous put mutants (put1-1 to put5-1) with Bc. Notably, put2-1 and put5-1 exhibited increased susceptibility to Bc, which was further exacerbated in the put2-1 put5-1 double mutant. Spermidine supplementation had a reduced effect on enhancing Bc resistance in put mutants, while it increased resistance in the 35S::PUT2 overexpression lines, suggesting that spermidine transport contributes to plant defense. Consistently, spermidine treatment elevated endogenous spermidine levels in WT but had minimal effect on put2-1, put5-1, or the double mutant. In contrast, spermine supplementation raised endogenous spermine levels in all genotypes, even under infection. Under mock conditions, catalase and ascorbate peroxidase activities were elevated in put mutants, while polyamine oxidase activity remained unchanged. These antioxidant enzymes and polyamine oxidase activity were induced upon Bc infection in WT but not in put mutants. Thus, disruptions in polyamine transport may affect their catabolism and the plant antioxidant response. This research emphasizes the importance of PUT-mediated polyamine transport in the plant's defense response to Bc.
- 26 July 2025
- Published by Springer Nature in Physiology and Molecular Biology of Plants
- Vol. 31 (7) , 1053-1069
The polyamine uptake transporters PUT2/LAT4 and PUT5/LAT5 contribute to Arabidopsis defense response against Botrytis cinerea
Under biotic stress, plant polyamine metabolism undergoes significant changes, including increased biosynthesis and catabolism, which lead to hydrogen peroxide production. However, the roles of polyamine mobilization and transport across membranes remain elusive. Arabidopsis thaliana encodes five Polyamine Uptake Transporters (PUT1-PUT5). In this study, we investigated the role of polyamine transport in Arabidopsis during its interaction with the necrotrophic fungus Botrytis cinerea (Bc). Fungal inoculation induced the expression of all PUT/LAT genes at different times throughout disease progression. To assess their contribution to defense, we challenged five homozygous put mutants (put1-1 to put5-1) with Bc. Notably, put2-1 and put5-1 exhibited increased susceptibility to Bc, which was further exacerbated in the put2-1 put5-1 double mutant. Spermidine supplementation had a reduced effect on enhancing Bc resistance in put mutants, while it increased resistance in the 35S::PUT2 overexpression lines, suggesting that spermidine transport contributes to plant defense. Consistently, spermidine treatment elevated endogenous spermidine levels in WT but had minimal effect on put2-1, put5-1, or the double mutant. In contrast, spermine supplementation raised endogenous spermine levels in all genotypes, even under infection. Under mock conditions, catalase and ascorbate peroxidase activities were elevated in put mutants, while polyamine oxidase activity remained unchanged. These antioxidant enzymes and polyamine oxidase activity were induced upon Bc infection in WT but not in put mutants. Thus, disruptions in polyamine transport may affect their catabolism and the plant antioxidant response. This research emphasizes the importance of PUT-mediated polyamine transport in the plant's defense response to Bc.
- Open Access
- 23 August 2023
- Published by MDPI AG in Fermentation
- Vol. 9 (9) , 781
Solid-State Fermentation of Green Tea Residues as Substrates for Tannase Production by Aspergillus niger TBG 28A: Optimization of the Culture Conditions
Tea (Camellia sinensis) is an evergreen shrub that is recognized worldwide for its functional properties. The current global production of green tea is approximately 5.3 million tons per year. Green tea processing has severely affected the generation of agro-industrial waste. One strategy for reducing waste accumulation is the revalorization of agro-industrial wastes via solid-state fermentation (SSF). The aim of this study was to valorize green tea processing residues to produce tannase under SSF using an endemic strain from Western Ghats, Aspergillus niger TBG 28A. SSF was performed in Erlenmeyer flasks with spent green tea leaves inoculated with spores of A. niger TBG 28A. Bioprocess optimization was carried out by employing the Box–Benkhen experimental design, achieving a high enzymatic yield of 246.82 (U/g). The present study shows the complexity of the degradation of tannins and the different patterns of expression of fungal tannase obtained from A. niger TBG 28 A. The enzyme was further purified to obtain a fold purification of 16.35% and a molecular mass of 150 kDa. Producing tannase with a novel strain of A. niger TBG 28A is an interesting strategy to revalorize green tea waste.
- 23 August 2023
- Published by MDPI AG in Fermentation
- Vol. 9 (9) , 781
Open AccessSolid-State Fermentation of Green Tea Residues as Substrates for Tannase Production by Aspergillus niger TBG 28A: Optimization of the Culture Conditions
Tea (Camellia sinensis) is an evergreen shrub that is recognized worldwide for its functional properties. The current global production of green tea is approximately 5.3 million tons per year. Green tea processing has severely affected the generation of agro-industrial waste. One strategy for reducing waste accumulation is the revalorization of agro-industrial wastes via solid-state fermentation (SSF). The aim of this study was to valorize green tea processing residues to produce tannase under SSF using an endemic strain from Western Ghats, Aspergillus niger TBG 28A. SSF was performed in Erlenmeyer flasks with spent green tea leaves inoculated with spores of A. niger TBG 28A. Bioprocess optimization was carried out by employing the Box–Benkhen experimental design, achieving a high enzymatic yield of 246.82 (U/g). The present study shows the complexity of the degradation of tannins and the different patterns of expression of fungal tannase obtained from A. niger TBG 28 A. The enzyme was further purified to obtain a fold purification of 16.35% and a molecular mass of 150 kDa. Producing tannase with a novel strain of A. niger TBG 28A is an interesting strategy to revalorize green tea waste.