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Effect of the Structural Modification of Plant Proteins as Microencapsulating Agents of Bioactive Compounds from Annatto Seeds (Bixa orellana L.)
by
Ciro Gomez, Gelmy
, Torres, Juan D.
, Delgado, Efren
, Velazquez, Víctor
, Quintero Quiroz, Julián
, Rojas, John
in
absorption
/ Acylation
/ Amino acids
/ Annatto
/ antioxidant
/ Backup software
/ Beans
/ Bioactive compounds
/ Biological activity
/ Bixa orellana
/ Calorimetry
/ Differential scanning calorimetry
/ Dyes
/ Efficiency
/ Emulsifiers
/ Encapsulation
/ enzymatic hydrolysis
/ Ethylenediaminetetraacetic acid
/ Food
/ Food industry
/ Food labeling
/ gelatinization temperature
/ Gelation
/ Gels
/ Hydrolysis
/ Hydrophilicity
/ Industrial development
/ isoelectric point
/ lentils
/ modification proteins
/ Molecular weight
/ Plant extracts
/ plants proteins
/ Protein structure
/ Proteins
/ Quinoa
/ Secondary structure
/ seed extracts
/ Seeds
/ Sodium
/ Solubility
/ soy protein
/ Statistical analysis
/ Structure-function relationships
/ Temperature
/ thiols
/ Viscoelasticity
2024
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Effect of the Structural Modification of Plant Proteins as Microencapsulating Agents of Bioactive Compounds from Annatto Seeds (Bixa orellana L.)
by
Ciro Gomez, Gelmy
, Torres, Juan D.
, Delgado, Efren
, Velazquez, Víctor
, Quintero Quiroz, Julián
, Rojas, John
in
absorption
/ Acylation
/ Amino acids
/ Annatto
/ antioxidant
/ Backup software
/ Beans
/ Bioactive compounds
/ Biological activity
/ Bixa orellana
/ Calorimetry
/ Differential scanning calorimetry
/ Dyes
/ Efficiency
/ Emulsifiers
/ Encapsulation
/ enzymatic hydrolysis
/ Ethylenediaminetetraacetic acid
/ Food
/ Food industry
/ Food labeling
/ gelatinization temperature
/ Gelation
/ Gels
/ Hydrolysis
/ Hydrophilicity
/ Industrial development
/ isoelectric point
/ lentils
/ modification proteins
/ Molecular weight
/ Plant extracts
/ plants proteins
/ Protein structure
/ Proteins
/ Quinoa
/ Secondary structure
/ seed extracts
/ Seeds
/ Sodium
/ Solubility
/ soy protein
/ Statistical analysis
/ Structure-function relationships
/ Temperature
/ thiols
/ Viscoelasticity
2024
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Effect of the Structural Modification of Plant Proteins as Microencapsulating Agents of Bioactive Compounds from Annatto Seeds (Bixa orellana L.)
by
Ciro Gomez, Gelmy
, Torres, Juan D.
, Delgado, Efren
, Velazquez, Víctor
, Quintero Quiroz, Julián
, Rojas, John
in
absorption
/ Acylation
/ Amino acids
/ Annatto
/ antioxidant
/ Backup software
/ Beans
/ Bioactive compounds
/ Biological activity
/ Bixa orellana
/ Calorimetry
/ Differential scanning calorimetry
/ Dyes
/ Efficiency
/ Emulsifiers
/ Encapsulation
/ enzymatic hydrolysis
/ Ethylenediaminetetraacetic acid
/ Food
/ Food industry
/ Food labeling
/ gelatinization temperature
/ Gelation
/ Gels
/ Hydrolysis
/ Hydrophilicity
/ Industrial development
/ isoelectric point
/ lentils
/ modification proteins
/ Molecular weight
/ Plant extracts
/ plants proteins
/ Protein structure
/ Proteins
/ Quinoa
/ Secondary structure
/ seed extracts
/ Seeds
/ Sodium
/ Solubility
/ soy protein
/ Statistical analysis
/ Structure-function relationships
/ Temperature
/ thiols
/ Viscoelasticity
2024
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Effect of the Structural Modification of Plant Proteins as Microencapsulating Agents of Bioactive Compounds from Annatto Seeds (Bixa orellana L.)
Journal Article
Effect of the Structural Modification of Plant Proteins as Microencapsulating Agents of Bioactive Compounds from Annatto Seeds (Bixa orellana L.)
2024
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Overview
This project studied the use of lentil protein (LP) and quinoa protein (QP) in their native and modified states as carrier material in the encapsulation process by the ionic gelation technique of annatto seed extract. Soy protein (SP) was used as a model of carrier material and encapsulated bioactive compounds, respectively. The plant proteins were modified by enzymatic hydrolysis, N acylation, and N-cationization to improve their encapsulating properties. Additionally, the secondary structure, differential scanning calorimetry (DSC), solubility as a function of pH, isoelectric point (pI), molecular weight (MW), the content of free thiol groups (SH), the absorption capacity of water (WHC) and fat (FAC), emulsifier activity (EAI), emulsifier stability (ESI), and gelation temperature (Tg) were assessed on proteins in native and modified states. The results obtained demonstrated that in a native state, LP (80.52% and 63.82%) showed higher encapsulation efficiency than QP (73.63% and 45.77%), both for the hydrophilic dye and for the annatto extract. Structural modifications on proteins improve some functional properties, such as solubility, WHC, FAC, EAI, and ESI. However, enzymatic hydrolysis on the proteins decreased the gels’ formation, the annatto extract’s encapsulated efficiency, and the hydrophilic dye by the ionic gelation method. On the other hand, the modifications of N-acylation and N-cationization increased but did not generate statistically significant differences (p-value > 0.05) in the encapsulation efficiency of both the annatto extract and the hydrophilic dye compared to those obtained with native proteins. This research contributes to understanding how plant proteins (LP and QP) can be modified to enhance their encapsulating and solubility properties. The better encapsulation of bioactive compounds (like annatto extract) can improve product self-life, potentially benefiting the development of functional ingredients for the food industry.
Publisher
MDPI AG
Subject
/ Annatto
/ Beans
/ Differential scanning calorimetry
/ Dyes
/ Ethylenediaminetetraacetic acid
/ Food
/ Gelation
/ Gels
/ lentils
/ Proteins
/ Quinoa
/ Seeds
/ Sodium
/ Structure-function relationships
/ thiols
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