Glêydison Amarante Soares
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
Glêydison Amarante Soares has a total of 42 co-authors. Here are the top co-authors by number of shared publications:
- Marcelo Franco
Biotransformation and Organic Biocatalysis Research Group, Department of Exact Sciences, Santa Cruz State University, 45654-370 Ilhéus, Brazil
6 shared publications - Iasnaia Maria de Carvalho Tavares
State University of Southwest Bahia
3 shared publications Nadabe dos Santos Reis
Centre of Technical-Science Training, Federal University of Southern Bahia (UFSB), Itabuna, Brazil
3 shared publicationsJulieta Rangel de Oliveira
Departament of Exact Sciences and Technology, State University of Santa Cruz, Ilhéus, Brazil
2 shared publications- Julieta Rangel de Oliveira
Biotransformation and Organic Biocatalysis Research Group, Department of Exact Sciences, State University of Santa Cruz, Ilhéus 45654-370, Bahia, Brazil
2 shared publications Aila Riany de Brito
Departament of Natural Sciences and Exact, State University of Southweast Bahia, Itapetinga, Brazil
1 shared publication
Latest Publications
- 7 October 2021
- Published by Wiley in Biotechnology and Applied Biochemistry
- Vol. 69 (5) , 2081-2090
High‐throughput screening for distinguishing nitrilases from nitrile hydratases in Aspergillus and application of a Box–Behnken design for the optimization of nitrilase
Nitrilases and nitrile hydratases/amidases hydrolyze nitriles into carboxylic acids and/or amides, which are used in industrial chemical processes. In the present study, 26 microorganisms, including yeasts and filamentous fungi, in a minimum solid mineral medium supplemented with glucose and phenylacetonitrile were screened to evaluate their biocatalytic potential. Of these microorganisms, five fungi of the genus Aspergillus were selected and subjected to colorimetry studies to evaluate the production and distinction of nitrilase and nitrile hydratase/amidase enzymes. Aspergillus parasiticus Speare 7967 and A. niger Tiegh. 8285 produced nitrilases and nitrile hydratase, respectively. Nitrilase optimization was performed using a Box–Behnken design (BBD) and fungus A. parasiticus Speare 7967 with phenylacetonitrile volume (μl), pH, and carbohydrate source (starch:glucose; g/g) as independent variables and nitrilase activity (U ml–1) as dependent variable. Maximum activity (2.97 × 10–3 U ml–1) was obtained at pH 5.5, 80 μl of phenylacetonitrile, and 15 g of glucose. A. parasiticus Speare 7967 showed promise in the biotransformation of nitriles to carboxylic acids.
- 7 October 2021
- Published by Wiley in Biotechnology and Applied Biochemistry
- Vol. 69 (5) , 2081-2090
High‐throughput screening for distinguishing nitrilases from nitrile hydratases in Aspergillus and application of a Box–Behnken design for the optimization of nitrilase
Nitrilases and nitrile hydratases/amidases hydrolyze nitriles into carboxylic acids and/or amides, which are used in industrial chemical processes. In the present study, 26 microorganisms, including yeasts and filamentous fungi, in a minimum solid mineral medium supplemented with glucose and phenylacetonitrile were screened to evaluate their biocatalytic potential. Of these microorganisms, five fungi of the genus Aspergillus were selected and subjected to colorimetry studies to evaluate the production and distinction of nitrilase and nitrile hydratase/amidase enzymes. Aspergillus parasiticus Speare 7967 and A. niger Tiegh. 8285 produced nitrilases and nitrile hydratase, respectively. Nitrilase optimization was performed using a Box–Behnken design (BBD) and fungus A. parasiticus Speare 7967 with phenylacetonitrile volume (μl), pH, and carbohydrate source (starch:glucose; g/g) as independent variables and nitrilase activity (U ml–1) as dependent variable. Maximum activity (2.97 × 10–3 U ml–1) was obtained at pH 5.5, 80 μl of phenylacetonitrile, and 15 g of glucose. A. parasiticus Speare 7967 showed promise in the biotransformation of nitriles to carboxylic acids.
- 1 August 2020
- Published by Springer Nature in Biomass Conversion and Biorefinery
- Vol. 12 (8) , 3133-3144
Production and biochemical characterization of halotolerant β-glucosidase by Penicillium roqueforti ATCC 10110 grown in forage palm under solid-state fermentation
- 1 August 2020
- Published by Springer Nature in Biomass Conversion and Biorefinery
- Vol. 12 (8) , 3133-3144
Production and biochemical characterization of halotolerant β-glucosidase by Penicillium roqueforti ATCC 10110 grown in forage palm under solid-state fermentation
- 11 November 2019
- Published by Springer Nature in Journal of Food Science and Technology
- Vol. 57 (4) , 1342-1350
Development of amperometric biosensor in modified carbon paste with enzymatic preparation based on lactase immobilized on carbon nanotubes
The variety of products derived from milk, without or with lactose, encourages the development of more effective analytical techniques that can be applied to the quality control of both the production line and the final products. Thus, in this work an efficient and minimally invasive method for the detection of lactose was proposed, using a biosensor containing the enzyme lactase (LAC) immobilised on carbon nanotubes (CNTs) that, when reacting with lactose, emit an electrochemical signal. This biosensor was connected to a potentiostat, and its electrochemical cell was composed of the following three electrodes: reference electrode (Ag/AgCl), auxiliary electrode (platinum wire), and working electrode (biosensor) on which graphite (carbon) paste (CP), CNTs, and LAC were deposited. The transmission electron microscopy and scanning electron microscopy were used in the characterisation of the composite morphology, indicating excellent interactions between the CNTs and LAC. The sensitivity of the CP/LAC/CNT biosensor was determined as 5.67 μA cm−2.mmol−1 L and detection limits around 100 × 10−6 mol L−1 (electrode area = 0.12 cm2) and an increase in the stability of the system was observed with the introduction of CNTs because, with about 12 h of use, there was no variation in the signal (current). The results indicate that the association between the CNTs and LAC favoured the electrochemical system. Graphic Abstract
- 11 November 2019
- Published by Springer Nature in Journal of Food Science and Technology
- Vol. 57 (4) , 1342-1350
Development of amperometric biosensor in modified carbon paste with enzymatic preparation based on lactase immobilized on carbon nanotubes
The variety of products derived from milk, without or with lactose, encourages the development of more effective analytical techniques that can be applied to the quality control of both the production line and the final products. Thus, in this work an efficient and minimally invasive method for the detection of lactose was proposed, using a biosensor containing the enzyme lactase (LAC) immobilised on carbon nanotubes (CNTs) that, when reacting with lactose, emit an electrochemical signal. This biosensor was connected to a potentiostat, and its electrochemical cell was composed of the following three electrodes: reference electrode (Ag/AgCl), auxiliary electrode (platinum wire), and working electrode (biosensor) on which graphite (carbon) paste (CP), CNTs, and LAC were deposited. The transmission electron microscopy and scanning electron microscopy were used in the characterisation of the composite morphology, indicating excellent interactions between the CNTs and LAC. The sensitivity of the CP/LAC/CNT biosensor was determined as 5.67 μA cm−2.mmol−1 L and detection limits around 100 × 10−6 mol L−1 (electrode area = 0.12 cm2) and an increase in the stability of the system was observed with the introduction of CNTs because, with about 12 h of use, there was no variation in the signal (current). The results indicate that the association between the CNTs and LAC favoured the electrochemical system. Graphic Abstract