Interactions of antinutrients mixtures with bovine serum albumin and its influence on in vitro protein digestibility

Kaspchak, Elaine; Bonassoli, Andrea Briones Gonçalves; Iwankiw, Patrícia Kanczewski; Kayukawa, Cíntia Tiemi Misugi; Igarashi‐Mafra, Luciana; Mafra, Marcos R.

doi:10.1016/j.molliq.2020.113699

Cited by 6 publications

(18 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, TA can also initiate protein cross-linkages to form precipitates. 10,24,25 The current study shows that this phenomenon depends on the concentration of TA present. From the vast decrease (36.3%) observed from LPTA 0.1% to LPTA 0.5%, a high concentration of TA seems to facilitate this process.…”

Section: ■ Results and Discussionmentioning

confidence: 54%

“…(2020) observed an increase in turbidity of TA/BSA mixtures as the concentration of TA increased. 10 The initial step of the complexation process involves hydrophilic bonding of TA hydroxyl groups to polar groups of the protein to produce possibly soluble particles, thus leaving a less hydrophilic covering on the protein surface. Therefore, a subsequent interaction among complexes yields aggregates and precipitates.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…In a BSA−TA mixture, in vitro protein digestibility of BSA was also hindered significantly. 10 At 0.1% w/v TA, random hydrophobic stacking of LP and TA could have further obstructed peptic hydrolysis. 9 Gallotannin, which is a hydrolyzable tannin, has been reported to effectively inhibit enzymatic activity even at low concentrations, due to their high density and several hydroxyl groups.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…The effect of tannic acid on protein digestibility is influenced by the concentration of tannic acid present. 10 However, the native sequence and structure of proteins dictate the mechanism of protein−tannic acid interaction. 9,17 The evaluation of possible modifications that occur after lentil protein and tannic acid interaction and the resulting effect on their digestibility are relevant to understand the effect of the interaction on the protein's functionality and bioactivity.…”

Section: ■ Introductionmentioning

confidence: 99%

“…It can advance to a hydrophobic bonding to yield complexes that can be soluble or insoluble. At a favorable protein–tannic acid ratio and pH (around isoelectric point of the protein), insoluble complexes are formed due to reduced electrostatic interactions. − Although tannic acid binding might be nonspecific, net charge, conformation, and size influence protein binding. Conditions, such as temperature, ionic strength, pH, and concentration, are also essential. − The pH can affect the stability of the hydrophilic bond and be reversed.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Lentil Protein and Tannic Acid Interaction Limits in Vitro Peptic Hydrolysis and Alters Peptidomic Profiles of the Proteins

Boachie

Okagu

Abioye

et al. 2022

J. Agric. Food Chem.

View full text Add to dashboard Cite

In this study, the nature of lentil protein-tannic acid (LPTA) interaction and its effect on in vitro pepsin digestion were investigated. LPTA mixtures containing 1% w/v LP and 0.001–0.5% TA were prepared and characterized in terms of particle size, thermal properties, and secondary and tertiary structures. A 20-fold increase in particle size was observed in LPTA0.5% compared to LP control (without TA), indicating aggregation. Static quenching of tryptophan residues within the protein hydrophobic folds was observed. Increasing TA levels also enhanced protein thermal stability. Over 50% reduction in free amino groups of LPTA 0.5%, relative to LP, was observed after pepsin digestion. Cleavage specificity of pepsin and peptidomic profile of LP were modified by the presence of TA in LPTA 0.5%. This study showed that 0.5% w/v TA induced protein aggregation and reduced LP digestibility by hindering the accessibility of pepsin to the protein network, thus modifying the profile of released peptides.

show abstract

Section: ■ Results and Discussionmentioning

confidence: 54%

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Lentil Protein and Tannic Acid Interaction Limits in Vitro Peptic Hydrolysis and Alters Peptidomic Profiles of the Proteins

Boachie

Okagu

Abioye

et al. 2022

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

Encapsulation of flavonoids in foods for diabetics: The emerging paradigm for an effective therapy

Oliveira

Neri-Numa

Arruda

et al. 2022

Trends in Food Science & Technology

View full text Add to dashboard Cite

Antinutrient and Sugar Type Effect on Structure and Maillard Reaction of Bovine Serum Albumin Submitted to Mild Heating

Kaspchak

Igarashi‐Mafra

Mafra

2022

ACS Food Sci. Technol.

Self Cite

View full text Add to dashboard Cite

Maillard reaction (MR) monitoring is important in food processing and new material development for protein–carbohydrate conjugates. This work aimed to investigate the antinutrient (AN; phytic acid, tannic acid, and saponin) and sugar type (glucose, fructose, and xylose) effect on the bovine serum albumin (BSA) structure and thermal behavior. Circular dichroism, fluorescence, UV–vis spectrophotometry, and differential scanning calorimetry were used to evaluate protein structure and MR. Results showed that all ANs impact protein’s secondary and tertiary structure of glycated BSA. Tannic acid and saponin decreased the absorbance of BSA and sugar mixtures, showing their MR inhibition ability. Phytic acid presents a small impact on the BSA structure; however, a catalytic effect on MR is observed by the browning of the samples. Both antinutrients and BSA changed the thermal behavior of the evaluated sugars in solid-state mixtures. These results may help to understand the sugar type and antinutrient role in the BSA behavior observed during heating.

show abstract

Interactions of antinutrients mixtures with bovine serum albumin and its influence on in vitro protein digestibility

Cited by 6 publications

References 46 publications

Lentil Protein and Tannic Acid Interaction Limits in Vitro Peptic Hydrolysis and Alters Peptidomic Profiles of the Proteins

Lentil Protein and Tannic Acid Interaction Limits in Vitro Peptic Hydrolysis and Alters Peptidomic Profiles of the Proteins

Encapsulation of flavonoids in foods for diabetics: The emerging paradigm for an effective therapy

Antinutrient and Sugar Type Effect on Structure and Maillard Reaction of Bovine Serum Albumin Submitted to Mild Heating

Contact Info

Product

Resources

About