Ruann Janser Soares de Castro
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Ruann Janser Soares de Castro has a total of 162 co-authors. Here are the top co-authors by number of shared publications:
Hélia Harumi Sato
Laboratory of Food Biochemistry, Department of Food Science and Nutrition, School of Food Engineering, University of Campinas, São Paulo, Brazil
21 shared publications- André Ohara
B CUBE Center for Molecular Bioengineering, TU Dresden, 01307 Dresden, Germany
9 shared publications - Gabriela Boscariol Rasera
Universidade Estadual de Campinas, Brasil
9 shared publications - Hélia Harumi Sato
Universidade Estadual de Campinas
8 shared publications - Jessika Gonçalves dos Santos Aguilar
University of Campinas
8 shared publications - Francielle Miranda de Matos
Department of Food Science and Nutrition, School of Food Engineering University of Campinas Campinas SP Brazil
7 shared publications
Latest Publications
- 7 November 2026
- Published by Elsevier in Food and Humanity
- Vol. 7
Seriguela (Spondias purpurea L.): Linking phytochemistry, bioactive properties and food applications
- 7 November 2026
- Published by Elsevier in Food and Humanity
- Vol. 7
Seriguela (Spondias purpurea L.): Linking phytochemistry, bioactive properties and food applications
- Open Access
- 29 January 2026
- Published by Elsevier in Biocatalysis and Agricultural Biotechnology
- Vol. 72
How germination conditions modulate the enzymatic activities, antioxidant potential and phenolic profile of chickpeas
- 29 January 2026
- Published by Elsevier in Biocatalysis and Agricultural Biotechnology
- Vol. 72
Open AccessHow germination conditions modulate the enzymatic activities, antioxidant potential and phenolic profile of chickpeas
- Open Access
- 1 January 2026
- Published by FapUNIFESP (SciELO) in Anais da Academia Brasileira de Ciências
- Vol. 98 (3)
Comparative study of aqueous ultrasound-assisted extraction methods of bioactive compounds from Tarumã (Vitex megapotamica)
Vitex megapotamica (Tarumã) fruits are a potential source of phenolic compounds with relevant biological activities. This study compared ultrasound-assisted extraction (UAE) using a probe-type ultrasonic apparatus with conventional shaker extraction for the recovery of bioactive compounds from ripe Tarumã fruits. UAE extraction kinetics were evaluated at 5, 10, 15, and 30 min (90 °C, 60% amplitude). The extracts were evaluated for their highest total phenolic content (TPC), antioxidant, and anti-inflammatory activities. The TPC was obtained after 5 min of extraction, and this condition was selected for comparison with shaker extraction under the same parameters. UAE significantly increased phenolic recovery, reaching 1909.2 mg GAE 100 g⁻¹ of sample, whereas the shaker method yielded 1549.5 mg GAE 100 g⁻¹. Despite the higher phenolic extraction efficiency, antioxidant and anti-inflammatory activities did not differ significantly between extracts (p > 0.05). High-performance liquid chromatography analysis (HPLC) revealed ellagic acid as the predominant compound in the UAE extract, while myricetin was the major phenolic compound identified in the shaker extract. These results demonstrate that UAE is an efficient and rapid technique to enhance the recovery of phenolic compounds from Tarumã fruits, supporting its potential application in the development of bioactive extracts.
- 1 January 2026
- Published by FapUNIFESP (SciELO) in Anais da Academia Brasileira de Ciências
- Vol. 98 (3)
Open AccessComparative study of aqueous ultrasound-assisted extraction methods of bioactive compounds from Tarumã (Vitex megapotamica)
Vitex megapotamica (Tarumã) fruits are a potential source of phenolic compounds with relevant biological activities. This study compared ultrasound-assisted extraction (UAE) using a probe-type ultrasonic apparatus with conventional shaker extraction for the recovery of bioactive compounds from ripe Tarumã fruits. UAE extraction kinetics were evaluated at 5, 10, 15, and 30 min (90 °C, 60% amplitude). The extracts were evaluated for their highest total phenolic content (TPC), antioxidant, and anti-inflammatory activities. The TPC was obtained after 5 min of extraction, and this condition was selected for comparison with shaker extraction under the same parameters. UAE significantly increased phenolic recovery, reaching 1909.2 mg GAE 100 g⁻¹ of sample, whereas the shaker method yielded 1549.5 mg GAE 100 g⁻¹. Despite the higher phenolic extraction efficiency, antioxidant and anti-inflammatory activities did not differ significantly between extracts (p > 0.05). High-performance liquid chromatography analysis (HPLC) revealed ellagic acid as the predominant compound in the UAE extract, while myricetin was the major phenolic compound identified in the shaker extract. These results demonstrate that UAE is an efficient and rapid technique to enhance the recovery of phenolic compounds from Tarumã fruits, supporting its potential application in the development of bioactive extracts.
- Open Access
- 1 January 2026
- Published by FapUNIFESP (SciELO) in Brazilian Journal of Food Technology
- Vol. 29
Sustainable recovery of phenolics from mustard seeds and study of their antioxidant and antimicrobial properties
This study aimed to investigate the effects of pH and temperature on the recovery of phenolic compounds from germinated and non-germinated mustard seeds. For this purpose, a Central Composite Rotatable Design (CCRD) was applied to mustard from two species (Brassica nigra and Sinapis alba). The evaluated responses included total phenolic content (TPC), antioxidant (ABTS, DPPH, FRAP) and antimicrobial activities, as well as phenolic identification and quantification by HPLC-DAD. The most suitable pH and temperature conditions for obtaining extracts with higher TPC content and antioxidant activity, varied according to sample type: for non-germinated white mustard (pH 5 at 37.5 °C); for germinated white mustard (pH 7.1 at 46.4 °C); for non-germinated black mustard (pH 5 at 25 °C) and for germinated black mustard (pH 8 at 37.5 °C). Under optimized conditions, sinapic acid was identified as the major phenolic compound in all samples, ranging from 700 µg g-1 (non-germinated white mustard) to 1270 µg g-1 (germinated black mustard). Furthermore, all mustard extracts inhibited microbial growth to varying degrees depending on the bacterial strain and sample evaluated. Overall, the results highlight the potential of green extraction using pH adjustment and mild temperatures for the recovery of phenolic antioxidants with antimicrobial activities.
- 1 January 2026
- Published by FapUNIFESP (SciELO) in Brazilian Journal of Food Technology
- Vol. 29
Open AccessSustainable recovery of phenolics from mustard seeds and study of their antioxidant and antimicrobial properties
This study aimed to investigate the effects of pH and temperature on the recovery of phenolic compounds from germinated and non-germinated mustard seeds. For this purpose, a Central Composite Rotatable Design (CCRD) was applied to mustard from two species (Brassica nigra and Sinapis alba). The evaluated responses included total phenolic content (TPC), antioxidant (ABTS, DPPH, FRAP) and antimicrobial activities, as well as phenolic identification and quantification by HPLC-DAD. The most suitable pH and temperature conditions for obtaining extracts with higher TPC content and antioxidant activity, varied according to sample type: for non-germinated white mustard (pH 5 at 37.5 °C); for germinated white mustard (pH 7.1 at 46.4 °C); for non-germinated black mustard (pH 5 at 25 °C) and for germinated black mustard (pH 8 at 37.5 °C). Under optimized conditions, sinapic acid was identified as the major phenolic compound in all samples, ranging from 700 µg g-1 (non-germinated white mustard) to 1270 µg g-1 (germinated black mustard). Furthermore, all mustard extracts inhibited microbial growth to varying degrees depending on the bacterial strain and sample evaluated. Overall, the results highlight the potential of green extraction using pH adjustment and mild temperatures for the recovery of phenolic antioxidants with antimicrobial activities.
- 20 November 2025
- Published by Elsevier in Food Research International
- Vol. 223 (Pt 2) , 117898
Enzymatic production and proteomic identification of bioactive peptides with α-amylase and α-glucosidase inhibitory activities from Pleurotus spp. proteins
- 20 November 2025
- Published by Elsevier in Food Research International
- Vol. 223 (Pt 2) , 117898
Enzymatic production and proteomic identification of bioactive peptides with α-amylase and α-glucosidase inhibitory activities from Pleurotus spp. proteins
- Open Access
- 30 September 2025
- Published by Wiley in Journal of Food Science
- Vol. 90 (10) , e70595
Characterization and Identification of Potential Antioxidant, Antidiabetic, and Antihypertensive Peptides From Hydrolysates of Tenebrio molitor Flour and Its Protein Concentrate
Insects are recognized as a potential alternative source of proteins and have been studied in recent years as a substrate for enzymatic hydrolysis to obtain bioactive peptides. This study aimed to evaluate the production of hydrolysates with antioxidant, antidiabetic, and antihypertensive properties from mealworm ( Tenebrio molitor ) flour and its protein concentrate. The proteases flavourzyme, alcalase, and neutrase were used for hydrolysis, according to an experimental design of mixtures. The highest antioxidant properties for the mealworm flour were found in the control test, where the substrate remained non‐hydrolyzed. The mealworm protein concentrate hydrolysates treated with Flavourzyme exhibited the highest values for ABTS and DPPH radical scavenging activities. The hydrolysis of mealworm flour and its protein concentrate increased their inhibitory activities against α‐amylase, α‐glucosidase, and angiotensin‐converting enzyme. A significant ( p < 0.05) and positive correlation was observed between the profiles of protein solubilization ( R 2 > 0.96), free amino groups ( R 2 > 0.94), and antioxidant properties ( R 2 > 0.87) of the hydrolysates obtained from integral flour and of its protein concentrate, indicating that the enzyme action was maintained, despite the differences in substrate composition. The results showed that, in terms of the process, protein concentration is not essential for the production of hydrolysates with bioactive properties. The proteomic analysis identified 38 peptides in the < 3 kDa fraction of the mealworm concentrate protein hydrolyzed with Flavourzyme. These sequences were composed of fractions characterized as bioactive, and in silico analysis predicts some potential bioactive peptides, such as the sequence LPAIL.
- 30 September 2025
- Published by Wiley in Journal of Food Science
- Vol. 90 (10) , e70595
Open AccessCharacterization and Identification of Potential Antioxidant, Antidiabetic, and Antihypertensive Peptides From Hydrolysates of Tenebrio molitor Flour and Its Protein Concentrate
Insects are recognized as a potential alternative source of proteins and have been studied in recent years as a substrate for enzymatic hydrolysis to obtain bioactive peptides. This study aimed to evaluate the production of hydrolysates with antioxidant, antidiabetic, and antihypertensive properties from mealworm ( Tenebrio molitor ) flour and its protein concentrate. The proteases flavourzyme, alcalase, and neutrase were used for hydrolysis, according to an experimental design of mixtures. The highest antioxidant properties for the mealworm flour were found in the control test, where the substrate remained non‐hydrolyzed. The mealworm protein concentrate hydrolysates treated with Flavourzyme exhibited the highest values for ABTS and DPPH radical scavenging activities. The hydrolysis of mealworm flour and its protein concentrate increased their inhibitory activities against α‐amylase, α‐glucosidase, and angiotensin‐converting enzyme. A significant ( p < 0.05) and positive correlation was observed between the profiles of protein solubilization ( R 2 > 0.96), free amino groups ( R 2 > 0.94), and antioxidant properties ( R 2 > 0.87) of the hydrolysates obtained from integral flour and of its protein concentrate, indicating that the enzyme action was maintained, despite the differences in substrate composition. The results showed that, in terms of the process, protein concentration is not essential for the production of hydrolysates with bioactive properties. The proteomic analysis identified 38 peptides in the < 3 kDa fraction of the mealworm concentrate protein hydrolyzed with Flavourzyme. These sequences were composed of fractions characterized as bioactive, and in silico analysis predicts some potential bioactive peptides, such as the sequence LPAIL.
- Open Access
- 11 September 2025
- Published by Wiley in Journal of Food Science
- Vol. 90 (9) , e70554
Effects of Fermentation on the Bioactive, Functional, and Technological Characteristics of Babassu and Brazil Nut Flours
This study provides a comprehensive evaluation of the composition, bioactivity, and techno‐functional properties of babassu ( Attalea speciosa ) mesocarp and Brazil nut ( Bertholletia excelsa ) flours, highlighting their potential as novel functional ingredients. Fermentation effects of Saccharomyces cerevisiae var. boulardii ‐17 on these properties were also investigated. Yeast cells (10 8 cells mL −1 ) were inoculated into flour suspensions (100 mg mL −1 ), and samples were collected every 4 h over a 12‐h fermentation period. In babassu flour, fermentation increased protein content and reduced lipid and ash levels, whereas Brazil nut flour showed minimal compositional changes, except for a decrease in carbohydrates. Lysine content increased in both substrates after fermentation. Among fermented samples, the 12‐h fermented babassu flour showed the best results for antioxidant assays, reaching 92.76, 105.07, and 181.77 µmol TE g −1 for 2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulfonic acid) (ABTS), 2,2‐difenil‐1‐picrilhidrazil (DPPH), and ferric reducing antioxidant power (FRAP) methods, respectively. Brazil nut samples also showed improved antioxidant activity after 4 h, with DPPH and FRAP values of 6.48 and 11.77 µmol TE g −1 , respectively. For babassu, α‐glucosidase inhibition peaked after 8 h of fermentation (40.26%) and remained high after 12 h (35.87%). Fermentation enhanced the emulsifying capacity of Brazil nut flour, exceeding 74% from 4 h onward. Upon scale‐up, improvements in ABTS and DPPH scavenging activity, α‐glucosidase inhibition, and oil holding capacity were detected in babassu, whereas Brazil nut flour showed enhanced gelling properties. The results suggest the potential application of these fermented flours as functional ingredients in the formulation of plant‐based food products.
- 11 September 2025
- Published by Wiley in Journal of Food Science
- Vol. 90 (9) , e70554
Open AccessEffects of Fermentation on the Bioactive, Functional, and Technological Characteristics of Babassu and Brazil Nut Flours
This study provides a comprehensive evaluation of the composition, bioactivity, and techno‐functional properties of babassu ( Attalea speciosa ) mesocarp and Brazil nut ( Bertholletia excelsa ) flours, highlighting their potential as novel functional ingredients. Fermentation effects of Saccharomyces cerevisiae var. boulardii ‐17 on these properties were also investigated. Yeast cells (10 8 cells mL −1 ) were inoculated into flour suspensions (100 mg mL −1 ), and samples were collected every 4 h over a 12‐h fermentation period. In babassu flour, fermentation increased protein content and reduced lipid and ash levels, whereas Brazil nut flour showed minimal compositional changes, except for a decrease in carbohydrates. Lysine content increased in both substrates after fermentation. Among fermented samples, the 12‐h fermented babassu flour showed the best results for antioxidant assays, reaching 92.76, 105.07, and 181.77 µmol TE g −1 for 2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulfonic acid) (ABTS), 2,2‐difenil‐1‐picrilhidrazil (DPPH), and ferric reducing antioxidant power (FRAP) methods, respectively. Brazil nut samples also showed improved antioxidant activity after 4 h, with DPPH and FRAP values of 6.48 and 11.77 µmol TE g −1 , respectively. For babassu, α‐glucosidase inhibition peaked after 8 h of fermentation (40.26%) and remained high after 12 h (35.87%). Fermentation enhanced the emulsifying capacity of Brazil nut flour, exceeding 74% from 4 h onward. Upon scale‐up, improvements in ABTS and DPPH scavenging activity, α‐glucosidase inhibition, and oil holding capacity were detected in babassu, whereas Brazil nut flour showed enhanced gelling properties. The results suggest the potential application of these fermented flours as functional ingredients in the formulation of plant‐based food products.
- Open Access
- 2 September 2025
- Published by American Chemical Society (ACS) in ACS Food Science & Technology
- Vol. 5 (9) , 3520-3529
First-Order Degradation Kinetics of Phenolic Compounds and Antioxidant Properties of Fresh and Enzymatically Hydrolyzed Seriguela Pulp (Spondias purpurea L.)
- 2 September 2025
- Published by American Chemical Society (ACS) in ACS Food Science & Technology
- Vol. 5 (9) , 3520-3529
Open AccessFirst-Order Degradation Kinetics of Phenolic Compounds and Antioxidant Properties of Fresh and Enzymatically Hydrolyzed Seriguela Pulp (Spondias purpurea L.)
- 2 May 2025
- Published by Elsevier in Biocatalysis and Agricultural Biotechnology
- Vol. 66
Transforming insects into a conventional food source using biotechnological processes
- 2 May 2025
- Published by Elsevier in Biocatalysis and Agricultural Biotechnology
- Vol. 66
Transforming insects into a conventional food source using biotechnological processes
- 28 March 2025
- Published by Springer Nature in Current Food Science and Technology Reports
- Vol. 3 (1) , 1-11
Advances in High-Pressure Homogenization for Plant Proteins: Enhancing Techno-Functional Properties and Bioactive Peptide Release
- 28 March 2025
- Published by Springer Nature in Current Food Science and Technology Reports
- Vol. 3 (1) , 1-11
Advances in High-Pressure Homogenization for Plant Proteins: Enhancing Techno-Functional Properties and Bioactive Peptide Release