Microencapsulation of casein hydrolysates: Physicochemical, antioxidant and microstructure properties

Sarabandi, Khashayar; Mahoonak, Alireza Sadeghi; Hamishekar, Hamed; Ghorbani, Mohammad; Jafari, Seid Mahdi

doi:10.1016/j.jfoodeng.2018.05.036

Cited by 108 publications

(54 citation statements)

References 55 publications

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“…tion of more soluble products[Klompong et al, 2017], since smaller peptides have increased the accessibility of hydrophilic groups, and facilitated the reaction of hydrophilic amino acid to the aqueous medium[Nguyen et al, 2017;Sarabandi et al, 2018]. The high solubility of the peptides obtained via ultra ltration using molecular weight cut-off membranes is presumably caused by the exposure of all hydrophilic groups of small molecules to the aqueous environment[Wu …”

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Functional Properties of Enzymatic Hydrolysate and Peptide Fractions from Perilla Seed Meal Protein

Park

Yoon

2019

Pol. J. Food Nutr. Sci.

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Córdova-Murueta & García-Carreño, 2002]. Hydrolysates containing low molecular weight peptides are easier to digest and absorb than long polymeric proteins and are widely available in various foods and processed products [Megias et al., 2009]. Peptides produced via enzymatic hydrolysis of food proteins exhibit physicochemical properties that are different from those of the original proteins because of lower molecular weights and exposure of hydrophobic residues caused by changes in the molecular structure, while maintaining physiological activity. Peptides present in food products exert biological control functions and provide nutritional value by supplying amino acids. In addition, peptides have excellent emulsifying properties and desired physical properties, such as gel-forming ability, solubility, viscosity, and emulsion properties, and strong af nity fat, and are thus ideal components of food products, such as sports drinks, dietetic foods, and health supplements [Chalamaiah et al., 2012; Benitez et al., 2008]. Various bioactive peptides have been produced from proteins, and their potential use as a functional food material has been proposed. Therefore, in the present study, PSM protein hydrolysate was prepared via enzymatic degradation, and the peptides from the hydrolysate were fractionated based on the molecular weight using an ultra ltration system. The amino acid composition and physical properties, including solubility, emulsi cation, foaming, oil retention, and water absorption properties, of the protein hydrolysate and peptide fractions were evaluated to serve as the basis for the utilization of PSM as functional ingredients in food products.

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confidence: 99%

Functional Properties of Enzymatic Hydrolysate and Peptide Fractions from Perilla Seed Meal Protein

Park

Yoon

2019

Pol. J. Food Nutr. Sci.

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“…Partículas obtidas por spray drying são geralmente esferas ocas, e a formação de vacúolos pode ser causada pelo processo de encolhimento que ocorre após o endurecimento da superfície externa, seguido pela expansão das bolhas de ar que estão presas dentro da gotícula, pulverizadas na câmara de secagem. Os mecanismos associados à formação de vazios estão relacionados com a expansão das partículas durante os últimos estágios do processo de secagem (Sarabandi et al, 2018).…”

Section: Microestrutura Dos Pósunclassified

“…No período estudado, foi possível notar que os materiais apresentaram boa manutenção da capacidade antioxidante, mesmo sem a proteção do material de parede, acima de 80% nos três casos. Sarabandi et al (2018) obtiveram hidrolisados de caseína utilizando alcalase e pancreatina e microencapsularam com maltodextrina. Os autores observaram que, mesmo após o processo de microencapsulação, os pós de caseína hidrolisados mantiveram a capacidade antioxidante pelo método ABTS em 77,5% e 91,6%, respectivamente.…”

Section: Avaliação Da Cor E Capacidade Antioxidanteunclassified

“…Diversos biopolímeros podem ser utilizados como material de parede (Sarabandi et al, 2018). Maltodextrina, goma arábica, proteínas e amidos modificados são agentes encapsulantes utilizados com frequência (Costa et al, 2015a(Costa et al, , 2015bHoyos-Leyva et al, 2018;Souza et al, 2018).…”

Section: Introductionunclassified

“…Uma das limitações da utilização das proteínas hidrolisadas em produtos alimentares é o seu gosto amargo, o qual está relacionado à formação de pequenos peptídeos compostos, principalmente, de aminoácidos hidrofóbicos (Adler-Nissen, 1986). Alguns autores como Sarabandi et al (2018) e Subtil et al (2014) aplicaram a tecnologia de microencapsulação para mascarar o gosto amargo.…”

Section: Introductionunclassified

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Estabilidade física e química de hidrolisados proteicos de okara microencapsulados por spray drying

Justus

Benassi

Ida

et al. 2020

Braz. J. Food Technol.

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Resumo A microencapsulação é um processo indicado para proteger substâncias que são susceptíveis à degradação ou redução da sua funcionalidade por causa de diferentes reações, por exemplo, oxidação, hidrólise, entre outras. O objetivo deste estudo foi avaliar o efeito da microencapsulação, usando como materiais de parede maltodextrina ou amido modificado, sobre a estabilidade de hidrolisados proteicos de okara. A pesquisa analisou a microestrutura, a capacidade antioxidante e a cor das amostras durante a estocagem dos pós por 120 dias a 35 °C. As micrografias obtidas por microscopia eletrônica de varredura indicaram que o processo de microencapsulação favoreceu a integridade física das partículas. A diferença de cor observada entre as amostras encapsuladas e não encapsuladas foi proveniente, provavelmente, da adição de materiais de paredes que contribuíram para a mudança da cor do pó obtido por spray drying. Os resultados indicaram que as microcápsulas obtidas por spray drying usando maltodextrina ou amido modificado mantiveram a cor dos pós e apresentaram boa habilidade em sequestrar o radical livre ABTS e teor de substâncias redutoras do reagente Folin-Ciocalteu durante a estocagem.

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Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

et al. 2022

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The interaction of one anticancer drug (caffeic acid phenethyl ester; CAPE) with three proteases (trypsin, pepsin and α-chymotrypsin) has been investigated with multispectral methods and molecular docking. As an active components in propolis, the findings are of great benefit to metabolism, design, and structural modification of drugs. The results show that CAPE has an obvious ability to quench the trypsin, pepsin, or α-chymotrypsin fluorescence mainly through a static quenching procedure.Trypsin has the largest binding affinity to CAPE, and α-chymotrypsin has the smallest binding affinity to CAPE. The data obtained from thermodynamic parameters and molecular docking prove that the spontaneously interaction between CAPE and each protease is mainly due to a combination of van der Waals (vdW) force and hydrogen bond (H-bond), controlled by an enthalpy-driven process. The binding force, strength, position, and the number of H-bond are further obtained from the results of molecular docking. Through ultraviolet spectroscopy, dynamic light scattering and circular dichroism experiments, the change in the protease secondary structure induced by CAPE was observed. Additionally, the addition of protease had a positive effect on the antioxidative activity of CAPE, and α-chymotrypsin has the greatest effect on the removal of 2,2-diphenyl-1-picrylhydrazyl free radicals by CAPE.α-chymotrypsin, caffeic acid phenethyl ester (CAPE), pepsin, trypsin | INTRODUCTIONCaffeic acid phenethyl ester (CAPE) has been widely used in various regions as a traditional natural medicine. [1] As the main active ingredient of propolis, CAPE has various biological activities, including anticancer, anti-inflammatory, antibacterial, neuroprotective, etc. [2][3][4] In addition, it has a very strong antioxidant capacity, [5] as a polyphenol containing hydroxyl groups in benzenediol. [6] In previous works, the study of the interaction between CAPE and macromolecules mainly focus on the binding mechanism, influencing factors, drug activities, and pharmacology; many theoretical researches have been done.Studies have shown that poly(3-hydroxybutyrate) (PHB) fibre can enhance the antioxidant and antibacterial activities of CAPE. [7] CAPE can inhibit iNOS gene transcription by inhibiting the nuclear factor NF-κB site, and can inhibit the catalytic activity of iNOS, [8] which provides a research basis for the anti-inflammatory and antitumour effects of CAPE. According to reports, after CAPE is compounded with γ-cyclodextrin (γ-CD), the anticancer activity of CAPE will increase. [9] In addition, in the work of this research group, the binding constant of CAPE and bovine serum albumin was $10 6 , of which the main forces are H-bond and vdW force, and the driving mode is enthalpy drive. However, there are few studies on the interaction

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Microencapsulation of casein hydrolysates: Physicochemical, antioxidant and microstructure properties

Cited by 108 publications

References 55 publications

Functional Properties of Enzymatic Hydrolysate and Peptide Fractions from Perilla Seed Meal Protein

Functional Properties of Enzymatic Hydrolysate and Peptide Fractions from Perilla Seed Meal Protein

Estabilidade física e química de hidrolisados proteicos de okara microencapsulados por spray drying

Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

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