13 results on '"Francisco Nogueira"'
Search Results
2. High-intensity ultrasound treatment on casein: Pea mixed systems: Effect on gelling properties
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Luis Gustavo Lima Nascimento, Lucas Sales Queiroz, Heidi Olander Petersen, Rodolphe Marie, Naaman Francisco Nogueira Silva, Mohammed Amin Mohammadifar, Paulo Peres de Sá Peixoto Júnior, Guillaume Delaplace, Antônio Fernandes de Carvalho, and Federico Casanova
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Gelation ,Sustainability ,Pea protein ,Green technology ,Milk protein ,General Medicine ,Food Science ,Analytical Chemistry - Abstract
This study aimed to investigate the suitability of the application of high-intensity ultrasounds (HIUS) to improve the acid induced gelation of mixed protein systems formed by casein micelles (CMs) and pea. The protein suspensions were prepared in different protein ratios CMs: pea (100:0, 80:20, 50:50, 20:80, 0:100) at 8% (w/w) total protein concentration. In the suspensions, the ultrasound treatment produced an increase in solubility, surface hydrophobicity, and a decrease in the samples’ viscosity, with more remarkable differences in protein blends in which pea protein was the major component. However, the replacement of 20% of CMs for pea proteins highly affected the gel elasticity. Hence, the creation of smaller and more hydrophobic building blocks before acidification due to the HIUS treatment increased the elasticity of the gels up to 10 times. Therefore, high-intensity ultrasounds are a suitable green technique to increase the gelling properties of CMs: pea systems.
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- 2023
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3. Pereskia aculeata Miller as a Novel Food Source:A Review
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Naaman Francisco Nogueira Silva, Sérgio Henrique Silva, Daniel Baron, Isabelle Cristina Oliveira Neves, and Federico Casanova
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Functional properties ,Health (social science) ,Sustainable protein sources ,Ora-pro-nobis ,Mucilage ,Plant proteins ,Bioactive molecules ,Plant Science ,Health Professions (miscellaneous) ,Microbiology ,Food Science - Abstract
Pereskia aculeata Miller is an edible plant species belonging to the Cactaceae family. It has the potential to be used in the food and pharmaceutical industries due to its nutritional characteristics, bioactive compounds, and mucilage content. Pereskia aculeata Miller is native to the Neotropical region, where it is traditionally employed as food in rural communities, being popularly known as ‘ora-pro-nobis’ (OPN) or the Barbados gooseberry. The leaves of OPN are distinguished by their nontoxicity and nutritional richness, including, on a dry basis, 23% proteins, 31% carbohydrates, 14% minerals, 8% lipids, and 4% soluble dietary fibers, besides vitamins A, C, and E, and phenolic, carotenoid, and flavonoid compounds. The OPN leaves and fruits also contain mucilage composed of arabinogalactan biopolymer that presents technofunctional properties such as thickener, gelling, and emulsifier agent. Moreover, OPN is generally used for pharmacological purposes in Brazilian folk medicine, which has been attributed to its bioactive molecules with metabolic, anti-inflammatory, antioxidant, and antimicrobial properties. Therefore, in the face of the growing research and industrial interests in OPN as a novel food source, the present work reviews its botanical, nutritional, bioactive, and technofunctional properties, which are relevant for the development of healthy and innovative food products and ingredients.
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- 2023
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4. Colloidal and Acid Gelling Properties of Mixed Milk and Pea Protein Suspensions
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Isabelle Carolina Oliveira, Iuri Emmanuel de Paula Ferreira, Federico Casanova, Angelo Luiz Fazani Cavallieri, Luis Gustavo Lima Nascimento, Antônio Fernandes de Carvalho, and Naaman Francisco Nogueira Silva
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Acid gel ,Health (social science) ,dairy proteins ,caseins ,plant proteins ,protein beverages ,acid gel ,colloidal stability ,Caseins ,food and beverages ,Dairy proteins ,Plant proteins ,Plant Science ,Protein beverages ,Health Professions (miscellaneous) ,Microbiology ,Colloidal stability ,Food Science - Abstract
The present study aims to describe colloidal and acid gelling properties of mixed suspensions of pea and milk proteins. Mixed protein suspensions were prepared by adding pea protein isolate to rehydrated skimmed milk (3% w/w protein) to generate four mixed samples at 5, 7, 9, and 11% w/w total protein. Skimmed milk powder was also used to prepare four pure milk samples at the same protein concentrations. The samples were analyzed in regard to their pH, viscosity, color, percentage of sedimentable material, heat and ethanol stabilities, and acid gelling properties. Mixed suspensions were darker and presented higher pH, viscosity, and percentage of sedimentable material than milk samples. Heat and ethanol stabilities were similar for both systems and were reduced as a function of total protein concentration. Small oscillation rheology and induced syneresis data showed that the presence of pea proteins accelerated acid gel formation but weakened the final structure of the gels. In this context, the results found in the present work contributed to a better understanding of mixed dairy/plant protein functionalities and the development of new food products.
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- 2022
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5. Milk quality, production process and physicochemical characteristics of Porungo, an artisanal cheese from the state of Sao Paulo, Brazil
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Natan de Jesus Pimentel Filho, Antônio Fernandes de Carvalho, Naaman Francisco Nogueira Silva, Ketilin Siqueira de Aguiar, Iuri Emmanuel de Paula Ferreira, Caetano Afonso Lanzoni Troiani, and Alline Artigiani Lima Tribst
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0303 health sciences ,Food Handling ,030306 microbiology ,media_common.quotation_subject ,General Medicine ,Raw milk ,Product (business) ,03 medical and health sciences ,Agricultural science ,Milk ,Cheese ,Food Microbiology ,Animals ,Cattle ,Animal Science and Zoology ,Quality (business) ,Business ,Mozzarella cheese ,Brazil ,030304 developmental biology ,Food Science ,media_common - Abstract
Porungo is a traditional pasta filata cheese produced using raw milk throughout the southwest region of the state of São Paulo, Brazil. The objectives of this Research Communication were to evaluate the quality of raw milk used to make Porungo cheese, to characterize its production process, and to determine its chemical composition. The results showed that the raw milk met both Brazilian and international quality requirements. Chemically, Porungo can be classified as a medium to full fat semi-hard fresh cheese. Our study has allowed the first standards and regulations for Porungo to be established in Brazil. By virtue of this, the local producers are able to formalize their activity while consumers can have access to a safe and certified product.
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- 2020
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6. Interactions between caseins and food-derived bioactive molecules:A Review
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Antônio Fernandes de Carvalho, Naaman Francisco Nogueira Silva, Frédéric Gaucheron, Luis Gustavo Lima Nascimento, and Federico Casanova
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chemistry.chemical_classification ,animal structures ,Biomolecule ,Bioactive molecules ,Casein ,Caseins ,General Medicine ,Health benefits ,Analytical Chemistry ,delivery systems ,chemistry ,Biochemistry ,nanovehicle ,carrier ,Functional Food ,Animals ,Humans ,encapsulation ,SDG 7 - Affordable and Clean Energy ,Nutritive Value ,Protein Binding ,Food Science - Abstract
Caseins are recognized as safe for consumption, abundant, renewable and have high nutritional value. Casein molecules are found in different aggregation states and their multiple binding sites offer the potential for delivering biomolecules with nutritional and/or health benefits, such as vitamins, phytochemicals, fibers, lipids, minerals, proteins, peptides, and pharmaceutical compounds. In the present review, we highlight the interactions between caseins and food-derived bioactive molecules, with a special focus on the aggregation states of caseins and the techniques used to produce and study the particles used for delivering. Research on interactions between caseins-minerals and casein-pharmaceutical molecules are not included here. This review aims to support the development of new and innovative functional foods in which caseins can be used as designed delivery systems.
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- 2021
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7. Casein-based hydrogels: A mini-review
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Luis Gustavo Lima Nascimento, Antônio Fernandes de Carvalho, Naaman Francisco Nogueira Silva, Alvaro Vianna Novaes de Carvalho Teixeira, and Federico Casanova
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Casein ,Biocompatible Materials ,Nanotechnology ,macromolecular substances ,01 natural sciences ,complex mixtures ,Analytical Chemistry ,Mini review ,Drug Delivery Systems ,0404 agricultural biotechnology ,Animals ,Humans ,SDG 7 - Affordable and Clean Energy ,chemistry.chemical_classification ,Biomolecule ,010401 analytical chemistry ,technology, industry, and agriculture ,Caseins ,Biomaterial ,Hydrogels ,04 agricultural and veterinary sciences ,General Medicine ,Biocompatible material ,040401 food science ,0104 chemical sciences ,Hydrogel ,chemistry ,Food ,Self-healing hydrogels ,Drug delivery ,Encapsulation ,Food Science - Abstract
Casein-based hydrogels are biocompatible, biodegradable, renewable, easy to obtain, inexpensive, and non-toxic. They exist in different physicochemical states, e.g. particle hydrogels, which can be dived in suspensions or emulsions and macro hydrogels that are gel colloid type. These biomaterials have drawn increasing attention in recent years due to their abilities to form networks of different tensile strengths and to encapsulate, protect and release biomolecules. This mini-review outlines the recent advances in casein-based hydrogel research and the uses of casein-based hydrogels as drug delivery system for both hydrophobic and hydrophilic molecules. The food and biomedical potential along with possible future uses of the casein-based hydrogels are discussed throughout the document.
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- 2020
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8. Combined effect of transglutaminase and sodium citrate on the microstructure and rheological properties of acid milk gel
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Federico Casanova, Frédéric Gaucheron, Alvaro Vianna Novaes de Carvalho Teixeira, Luiz Antônio Minim, Guilherme Mendes da Silva, Naaman Francisco Nogueira Silva, Antônio Fernandes de Carvalho, Centro de Ciencias da Natureza, Universidade Federal de Sao Carlos, Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa (UFC), Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Departamento de Física, UFPR, and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)
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Tissue transglutaminase ,General Chemical Engineering ,microstructure ,microscopie confocale ,Acid milk gel ,confocal microscopy ,citrate de sodium ,transglutaminase ,chemistry.chemical_compound ,0404 agricultural biotechnology ,Sodium citrate ,Rheology ,protein-glutamine ³-glutamyltransferase ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,Confocal laser scanning microscopy ,Water holding capacity ,gel acide ,rhéologie ,Microstructure ,Trisodium citrate ,milk ,biology ,gel laitier ,microfiltration ,04 agricultural and veterinary sciences ,General Chemistry ,Transglutaminase ,lait ,040401 food science ,chemistry ,microstructure des aliments ,biology.protein ,rheology ,gel laitier acide ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,δ lactone ,Food Science ,Nuclear chemistry - Abstract
Combined effects of trisodium citrate (TSC), transglutaminase (Tgase) and heating were studied with relation to the mechanical properties of acid milk gels. Acidification of skimmed microfiltered milk samples was performed at 30 °C by addition of glucono – δ lactone to achieve final pH of 4.6 in 4 h. Increasing levels of TSC (0, 10 and 20 mM) were added to the samples, followed by addition of a constant level of Tgase (3 U/g of protein), and subsequent heating to 85 °C for 30 min. Prior to acidification, suspensions were analyzed in terms of amount of sedimentable material, hydration, hydrodynamic diameter (Dh) and ζ-potential (ζ) of the particles. Acid-induced gelation was studied using small deformation rheology followed by large deformation test. The water holding capacity of the gels (WHC) was performed at pH 4.6. Gels microstructure were investigated by confocal laser scanning microscopy at pH 4.6 and determination of mean pore size was performed by 2D-correlation analysis. Results showed that combined Tgase and TSC treatments had significant effect on rheological properties, WHC and gel microstructure. Higher stiffness of the gels was observed with Tgase and TSC at 10 mM, whereas a homogenous network distribution with smaller pore size was observed in the presence of Tgase and TSC at 20 mM.
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- 2018
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9. Micelas de caseína: dos monômeros à estrutura supramolecular
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Michele da Silva Pinto, Antônio Fernandes de Carvalho, Naaman Francisco Nogueira Silva, Frédéric Gaucheron, and Federico Casanova
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animal structures ,Casein ,02 engineering and technology ,Casein micelle ,Colloidal calcium phosphate ,β-caseína ,κ-casein ,κ-caseína ,Micela de caseína ,Fosfato de cálcio coloidal ,Proteínas do leite ,TX341-641 ,β-casein ,Nutrition. Foods and food supply ,0402 animal and dairy science ,αS1-casein ,Milk proteins ,αS1-caseína ,04 agricultural and veterinary sciences ,021001 nanoscience & nanotechnology ,040201 dairy & animal science ,αS2-casein ,αS2-caseína ,Caseína ,0210 nano-technology ,Food Science - Abstract
Resumo A importância primária das micelas de caseína reside no fato de que os processos empregados na transformação do leite em quaisquer de seus derivados dependem, direta ou indiretamente, de sua estabilidade ou de sua desestabilização controlada. Assim, o objetivo do presente trabalho é apresentar uma revisão atualizada sobre a organização estrutural das micelas de caseína. Em termos físico-químicos, as micelas de caseína podem ser definidas como agregados supramoleculares esféricos e porosos, altamente hidratados, carregados negativamente, com diâmetro médio de 200 nm, e que apresentam aproximadamente 104 cadeias polipeptídicas. Além de água, as micelas são constituídas por quatro tipos de caseínas, chamadas de αS1, αS2, β, e κ-caseínas, que estão unidas por meio de interações hidrofóbicas e eletrostáticas, e pela presença de minerais, sobretudo sais de fosfato de cálcio, os quais são os principais responsáveis pela manutenção da estrutura micelar. A estabilidade das micelas de caseína é atribuída à presença de uma camada externa difusa, formada basicamente por κ-caseína. Apesar de as propriedades coloidais das micelas de caseína serem conhecidas, ainda não há consenso sobre como as moléculas de caseína estão estruturadas em seu interior. Portanto, os principais modelos que descrevem a organização interna das micelas de caseína são apresentados na parte final do artigo. Abstract The most relevant aspect concerning casein micelles lies in the fact that all the procedures employed in the transformation of milk into dairy products depend, directly or indirectly, on their stability or their controlled destabilization. Thus, the present paper aimed to present an updated review of the structural organization of casein micelles. Physicochemically, casein micelles can be defined as spherical, porous supramolecular aggregates, highly hydrated, negatively charged, with a mean diameter of about 200 nm, and presenting approximately 104polypeptide chains. Besides water, casein micelles are constituted of four types of casein molecule, namely αS1, αS2, β and κ-caseins, which are held together by means of hydrophobic and electrostatic interactions, and by the presence of minerals, mainly composed of calcium phosphate salts, which are considered the main factor responsible for maintaining the micellar structure. The stability of the casein micelles is attributed to the presence of an outer diffuse layer, basically composed of κ-casein. Although the colloidal properties of casein micelles are well known, there is still no consensus concerning their internal structure. Therefore, the main models describing the internal organization of casein micelles are presented in the final part of this article.
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- 2019
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10. Use of a crosslinked casein micelle hydrogel as a carrier for jaboticaba (Myrciaria cauliflora) extract
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De Sa Peixoto, P., Nascimento, Luis Gustavo Lima, Casanova, Federico, Silva, Naaman Francisco Nogueira, Teixeira, Álvaro Viana Novaes de Carvalho, Júnior, Paulo Peres de Sá Peixoto, Vidigal, Márcia Cristina Teixeira Ribeiro, Stringheta, Paulo Cesar, Carvalho, Antônio Fernandes de, Processus aux Interfaces et Hygiène des Matériaux (PIHM), Institut National de la Recherche Agronomique (INRA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Technical University of Denmark [Lyngby] (DTU), Centro de Ciencias da Natureza, Universidade Federal de Sao Carlos, Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa (UFC), and National Council for Scientific and Technological Development (CNPq) Minas Gerais State Research Foundation (FAPEMIG) CAPES001
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030309 nutrition & dietetics ,General Chemical Engineering ,Casein micelles ,Micelle ,Anthocyanins ,03 medical and health sciences ,0404 agricultural biotechnology ,Rheology ,Casein ,[CHIM]Chemical Sciences ,Jaboticaca crude extract ,[PHYS.COND]Physics [physics]/Condensed Matter [cond-mat] ,ComputingMilieux_MISCELLANEOUS ,[PHYS]Physics [physics] ,chemistry.chemical_classification ,0303 health sciences ,technology, industry, and agriculture ,Release profile ,04 agricultural and veterinary sciences ,General Chemistry ,Transglutaminase ,040401 food science ,Hydrogel ,Enzyme ,Polymerization ,chemistry ,13. Climate action ,Ultrapure water ,Self-healing hydrogels ,Lactone ,Food Science ,Nuclear chemistry - Abstract
Casein micelle hydrogels were developed using transglutaminase (Tgase) as a crosslink agent in order to encapsulate anthocyanins from jaboticaba fruit (Myrciaria cauliflora). Spray dried casein micelles (CMs) powder was rehydrated in ultrapure water at a concentration of 4.5% w/w, and Tgase was added at 3 units/g of casein. The suspensions were incubated at 45 °C for 1 h, followed by enzyme deactivation at 85 °C for 5 min. Jaboticaba extract (JE), obtained from jaboticaba peel, was added to the suspensions at a concentration of 2% (w/w) at 25 °C. In the suspensions, Tgase promoted a reduction in CMs size and an increase in the degree of casein polymerization. The presence of JE did not affect CMs size or charge. The hydrogel samples were produced by acidification of the suspensions using 2% w/w of glucono – δ – lactone until pH 4.5 at 30 °C. The hydrogels were analyzed using small deformation rheology and confocal laser scanning microscopy. Tgase treatment promoted the formation of a more compact protein matrix compared to the samples without the enzyme. The presence of JE decreased hydrogel elasticity and increased hydrogel pore size. The JE release profile was evaluated by immersing the hydrogels in three buffer solutions at pH 2.0, 4.5 and 7.0. The release rates for the hydrogels with Tgase were lower for all pH values. Solutions with higher pH values induced faster release rates. These findings can be applied to specific delivery systems, such as the transport of JE in an intestinal environment.
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- 2020
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11. Stability of casein micelles cross-linked with genipin: A physicochemical study as a function of pH
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Marcio H. Nogueira, Alvaro Vianna Novaes de Carvalho Teixeira, Frédéric Gaucheron, Maura P. Alves, Ítalo Tuler Perrone, Naaman Francisco Nogueira Silva, Antônio Fernandes de Carvalho, Federico Casanova, Priscila Cardoso Fidelis, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Department of Food Technology, Universidade Federal de Vicosa (UFV), Centre of Natural Sciences, Universidade Federal de São Carlos, Departemento de Fisica, and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)
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technologie laitière ,FOS: Physical sciences ,micelle de caséine ,Condensed Matter - Soft Condensed Matter ,Function of pH ,Applied Microbiology and Biotechnology ,Micelle ,Stability of casein micelles cross-linked ,produit laitier ,chemical stability ,chemistry.chemical_compound ,génipine ,0404 agricultural biotechnology ,Dynamic light scattering ,milk protein ,protéine du lait ,Casein ,health services administration ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,Physics - Biological Physics ,stabilité ,health care economics and organizations ,Ethanol ,Chromatography ,précipitation ,Precipitation (chemistry) ,0402 animal and dairy science ,méthode de précipitation à l'éthanol ,Biomolecules (q-bio.BM) ,04 agricultural and veterinary sciences ,040401 food science ,040201 dairy & animal science ,stabilité chimique ,Isoelectric point ,chemistry ,Quantitative Biology - Biomolecules ,Biological Physics (physics.bio-ph) ,FOS: Biological sciences ,Genipin ,Soft Condensed Matter (cond-mat.soft) ,Chemical stability ,propriété physicochimique du lait ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,Food Science - Abstract
Chemical or enzymatic cross-linking of casein micelles (CMs) increases their stability against dissociating agents. In this paper, a comparative study of stability between native CMs and CMs cross-linked with genipin (CMs-GP) as a function of pH is described. Stability to temperature and ethanol were investigated in the pH range 2.0-7.0. The size and the charge ($\zeta$-potential) of the particles were determined by dynamic light scattering. Native CMs precipitated below pH 5.5, CMs-GP precipitated from pH 3.5 to 4.5, whereas no precipitation was observed at pH 2.0-3.0 or pH 4.5-7.0. The isoelectric point of CMs-GP was determined to be pH 3.7. Highest stability against heat and ethanol was observed for CMs-GP at pH 2, where visible coagulation was determined only after 800 s at 140 $^\circ$C or 87.5% (v/v) of ethanol. These results confirmed the hypothesis that cross-linking by GP increased the stability of CMs., Comment: 5 pages, 2 figures, International Dairy Journal, 2016
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- 2017
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12. AFM study of casein micelles cross-linked by genipin: effects of acid pH and citrate
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Asma Bahri, Frédéric Gaucheron, Eric Beaucher, Fanny Guyomarc'H, Naaman Francisco Nogueira Silva, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)
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Inorganic chemistry ,Ingénierie des aliments ,chemistry.chemical_element ,micelle de caséine ,macromolecular substances ,Calcium ,Biochemistry ,Micelle ,produit laitier ,Contact angle ,microscopie à force atomique ,acidification ,chemistry.chemical_compound ,Colloid ,génipine ,Casein ,health services administration ,Sodium citrate ,micelle ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,Food engineering ,Food and Nutrition ,colloïde ,colloide ,citrate ,caséine ,calcium ,health care economics and organizations ,phosphate de calcium ,technology, industry, and agriculture ,Demineralization ,chemistry ,Chemical engineering ,13. Climate action ,Alimentation et Nutrition ,Genipin ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,Food Science - Abstract
This paper is part of the special issue dedicated to the 2nd International Symposium on Minerals & DairyProducts (MADP2014) held on 26–28th February 2014 in Auckland, New Zealand.; Casein micelles (CMs) are supramolecular structures highly dependent on their mineral content, especially colloidal calcium phosphate. When colloidal calcium phosphate is removed, the micellar structures dissociate and release minerals and casein molecules in the continuous phase. The aim of this work was to study the effects of solubilization of the colloidal calcium phosphate induced by acidification or addition of sodium citrate (100 mmol.L−1) on the structure of cross-linked CMs using atomic force microscopy (AFM). AFM was used to determine the dimensional characteristics, height, diameter, and contact angle of control and cross-linked CMs. To this end, micellar suspensions were cross-linked by genipin and then acidified or demineralized. Colloidal calcium was solubilized, and the results showed that the cross-linked CMs retained more calcium than control CMs. The AFM analysis revealed that control CMs were deformed after immobilization and shrunk upon acidification. As control CMs dissociated in the presence of citrate, dimensional characteristics were not determined by AFM. The crosslinked CMs were also deformed on immobilization but to a lesser extent than control ones. The dimensional characteristics of cross-linked CMs were not modified by acidification. Conversely, demineralization by citrate induced structural rearrangement of the micellar structures. The higher structural resistance of cross-linked CMs was related to intramicellar cross-links between basic amino acids (lysyl and arginyl residues) present in casein molecules. Although AFM was performed in the air, it allowed us to know how the ionic environment modulates the intrinsic nanomechanical properties of CMs.
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- 2015
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13. pH-induced demineralization of casein micelles modifies their physico-chemical and foaming properties
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Naaman Francisco Nogueira Silva, Frédéric Gaucheron, Frédéric Violleau, Anne-Laure Fameau, Michel Piot, Antônio Fernandes de Carvalho, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Departemento de Technologia de Alimentos, Laboratorio de Leite e Derivados, Universidade Federal de Vicosa (UFV), Département Sciences Agronomiques et Agroalimentaires - EI Purpan, Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Région Bretagne ARED 6188, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université Toulouse III - Paul Sabatier (UT3)
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education.field_of_study ,Chromatography ,Chemistry ,General Chemical Engineering ,Population ,0402 animal and dairy science ,Ionic bonding ,04 agricultural and veterinary sciences ,General Chemistry ,040401 food science ,040201 dairy & animal science ,Micelle ,caséine micelle suspension acidification agrégation mousse ,Suspension (chemistry) ,Demineralization ,Colloid ,0404 agricultural biotechnology ,Chemical engineering ,Ionic strength ,Casein ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,education ,ultracentrifugation lait ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition ,Food Science - Abstract
The organization and functional properties of caseins are influenced by several factors like temperature, pH, ionic environment, ionic strength, casein type and organization. The objective of this work was to prepare suspensions of casein micelles with different mineralization states to study their new physico-chemical and foaming properties. The different suspensions were obtained after milk acidification at various pH values (6.7 as control and 6.4, 6.1, 5.8 and 5.5) and then dialyzed against milk ultrafiltrate to have similar pH values and ionic environment. Each suspension was characterized in terms of i. composition and distribution of minerals and casein molecules between continuous and colloidal phases, ii. physico-chemical characteristics (percentage of sedimentable material, turbidity, particle size distribution, state of aggregation of casein molecules, shape, charge and hydration) and iii. foaming properties (foaming capacity and foam stability). The obtained suspensions were progressively demineralized and partial dissociations of casein micelles were observed. The dissociated part corresponded to non-sedimentable particles by ultracentrifugation. These particles have average diameter of about 20–35 nm and molecular weight between 106 and 107 g mol−1. The proportion of this population smaller in size increased when the pH used to obtain the different casein suspensions was acid (6.7
- Published
- 2013
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