Trypsin inhibitors in xoconostle seeds (Opuntia joconostle Weber.)

Aguirrezabala-Cámpano, Teresa; Torres-Acosta, Reyna Ivonne; Blanco‐Labra, Alejandro; Mediola-Olaya, Ma. Elizabeth; Sinagawa-García, Sugey Ramona; Gutiérrez-Díez, Adriana; Torres-Castillo, Jorge Ariel

doi:10.1007/s13562-012-0152-z

Cited by 6 publications

(4 citation statements)

References 21 publications

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“…In comparison to this work, an isolated polypeptide from Chinese cabbage seeds inhibited trypsin with an IC 50 value of 8.5 µM [48]. However, the pea peptides are stronger chymotrypsin inhibitors when compared to the two protease-inhibitory peptides extracted from Opuntia joconostle Weber seeds, which were inactive against this enzyme [36].…”

Section: Discussionmentioning

confidence: 98%

“…This is because chymotrypsin activity is specific for peptide bonds where the carbonyl group is donated by aromatic amino acids, such as tyrosine, phenylalanine, and tryptophan, while trypsin catalyzes bonds with the carboxyl side donated by arginine and lysine [47]. A previous work also showed that peptides inhibited trypsin activity but not chymotrypsin [36]. Overall, the pea protein hydrolysates and peptide fractions are significantly ( p < 0.05) weaker trypsin and chymotrypsin inhibitors when compared to AEBSF, which is considered a standard protease inhibitor.…”

Section: Discussionmentioning

confidence: 99%

“…For example, food protein-derived peptides have been proven to have various physiological effects that include free radical scavenging, blood pressure reduction, immunomodulation, bone development, neuroprotection, and renoprotection [34]. However, with the exception of two recent works showing the inhibition of BBI by a cyclic nonapeptide [35] and 4 kDa seed peptides [36], information is scant regarding serine protease inhibition by low molecular weight peptides, especially from enzymatic digests of food proteins. Therefore, we hypothesized in this study that peptides with inhibitory activities against trypsin and chymotrypsin can be isolated after hydrolysis of pea protein with alcalase, pepsin, trypsin, and chymotrypsin.…”

Section: Introductionmentioning

confidence: 99%

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Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

Awosika

Aluko

2019

Foods

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In this work, we report the potency of enzymatic hydrolysates of pea proteins against trypsin and chymotrypsin. Pea protein concentrate was digested with each of alcalase, chymotrypsin, pepsin, and trypsin, followed by membrane separation of the protein hydrolysates into peptide fractions (<1, 1–3, 3–5, and 5–10 kDa). Peptide size profiling with size-exclusion gel chromatography indicated the narrowest size range (0.85–4.98 kDa) for alcalase. Trypsin activity was strongly (p < 0.05) inhibited by the ultrafiltration fractions (mean IC50 = 2.2 mg/mL) obtained from the trypsin hydrolysate when compared to the unfractionated hydrolysate (IC50 = 6.8 mg/mL). Similarly, ultrafiltration also enhanced trypsin inhibition by the alcalase-digested peptides with an IC50 of 21.4 mg/mL for the unfractionated hydrolysate in comparison to 3.1–4.7 mg/mL for the fractions. However, ultrafiltration did not enhance trypsin inhibitory activity of chymotrypsin-digested peptides, while the peptide separation reduced efficacy of pepsin-digested peptides. In contrast, chymotrypsin inhibition by all the enzymatic digests was significantly (p < 0.05) enhanced by ultrafiltration, especially peptide sizes >3 kDa. Kinetics of enzyme inhibition indicate peptides were bound to the enzyme active site in a competitive mode that led to reduced catalysis. We conclude that the pea peptides could function as useful tools to promote human health and as a preservative during food processing and storage.

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

Awosika

Aluko

2019

Foods

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“…Hydrosoluble proteins were extracted by protocols of Aguirrezabala-Cámpano et al (2012), shaking 50 g of CAL flour at a ratio of 1:4 weight/volume (w/v) in distilled water at 4°C for 30 minutes. Subsequently, the mixture was centrifuged at 6,000 × g at 25-30°C for 10 minutes.…”

Section: Methodsmentioning

confidence: 99%

Potential Use of Central American Locust, Schistocerca piceifrons piceifrons1, as Food

Garza-Sánchez,

Torres-Castillo,

Barrientos-Lozano

et al. 2023

Southwestern Entomologist

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The Central American locust (CAL), Schistocerca piceifrons piceifrons (Walker) (Acrididae: Cyrtacanthacridinae), is a harmful agricultural pest from Mexico to Costa Rica. This study assessed the nutritional contents of the locust. Enzymatic digestibility of hydrosoluble proteins and the antioxidant capacities of the derived peptides were analyzed. Locust flour was used to make corn tortillas to analyze the water retention and physical properties of the tortillas. Protein content was 72.4%, and protein extract yielded 4.77 ± 0.095 mg per gram of dry weight. Trypsin provided the strongest protein digestion at 1 and 3 hours, compared to pepsin. Regarding peptide scavenging ability of free radicals, digestion with trypsin allowed detection of 0.068 and 0.055 mM TE/mg of protein, at digestive times of 1 and 3 hours, respectively. Overall, results were not statistically different. Corn tortillas displayed changes in color and consistency related to quantity of locust flour. When more locust flour was used, more water was lost during the cooking process. The research documents the potential of Central American locust as a protein source and brings the possibility of using this undervalued natural resource. Nutritional content of the CAL were compared to that of other edible insects.Resumen. La langosta Centroamericana (LCA), Schistocerca piceifrons piceifrons (Walker) (Acrididae: Cyrtacanthacridinae), es una plaga agrícola dañina desde México hasta Costa Rica. Este estudio evaluó el contenido nutricional de la langosta. Se analizó la digestibilidad enzimática de las proteínas hidrosolubles y las capacidades antioxidantes de los péptidos derivados. Se utilizó harina de langosta para elaborar tortillas de maíz para analizar la retención de agua y las propiedades físicas de las tortillas. El contenido de proteína fue de 72,4% y el extracto de proteína produjo 4,77 ± 0,095 mg por gramo de peso seco. La tripsina proporcionó la digestión de proteínas más fuerte a 1 y 3 horas, en comparación con la pepsina. En cuanto a la habilidad captadora de péptidos de los radicales libres, la digestión con tripsina permitió detectar 0,068 y 0,055 mM TE/mg de proteína, con tiempos digestivos de 1 y 3 horas, respectivamente. En general, estos resultados no mostraron diferencias estadísticas. Las tortillas de maíz presentaron cambios en color y consistencia en

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Micropropagation, phytochemistry and biological activity of the critically endangered Mammillaria herrerae Werdermann

Song

Kang²,

et al. 2021

South African Journal of Botany

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Trypsin inhibitors in xoconostle seeds (Opuntia joconostle Weber.)

Cited by 6 publications

References 21 publications

Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors

Potential Use of Central American Locust, Schistocerca piceifrons piceifrons1, as Food

Micropropagation, phytochemistry and biological activity of the critically endangered Mammillaria herrerae Werdermann

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