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1.
J Dairy Sci ; 98(5): 3514-25, 2015 May.
Artigo em Inglês | MEDLINE | ID: mdl-25722000

RESUMO

The current study assessed the perceived value of food traceability in modern society by young consumers. After experiencing numerous recalls and food safety-related incidences, consumers are increasingly aware of the tools available to mitigate risks. Food traceability has been associated with food safety procedures for many years, but recent high-profile cases of food fraud around the world have given traceability a different strategic purpose. Focusing solely on dairy products, our survey results offer a glimpse of consumer perceptions of traceability as a means to preserve food integrity and authenticity. This study explored the various influences that market-oriented traceability has had on dairy consumers. For example, results show that if the dairy sector could guarantee that their product is in fact organic, 53.8% of respondents who often purchase organic milk would consider always purchasing traceable organic milk. This research produced a quantitative set of information related to the perceived value of food traceability, which could be useful for the creation and development of improved guidelines and better education for consumers. We discuss limitations and suggest areas for new research.


Assuntos
Qualidade de Produtos para o Consumidor/normas , Laticínios/normas , Comportamento do Consumidor , Feminino , Rotulagem de Alimentos/normas , Inocuidade dos Alimentos , Humanos , Masculino , Política Nutricional/legislação & jurisprudência , Percepção , Recall e Retirada de Produto , Adulto Jovem
2.
Food Funct ; 5(6): 1160-6, 2014 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-24686838

RESUMO

Numerous studies have demonstrated that tea catechins form complexes with milk proteins, especially caseins. Much less work has been conducted to understand the metabolic conversions of tea-milk complexes during gastro-duodenal digestion. The objective of this study was to determine the significance of this association on the digestibility of the milk proteins and on the bioaccessibility of the tea polyphenol epigallocatechin gallate (EGCG). An in vitro digestion model mimicking the gastric and duodenal phases of the human gastrointestinal tract was employed to follow the fate of the milk proteins during digestion and determine the bioefficacy of EGCG isolated or encapsulated with the caseins. The samples, before and after digestion, were tested using two parallel colonic epithelial cell lines, a normal line (4D/WT) and its cancerous transformed counterpart (D/v-src). EGCG caused a decrease in proliferation of cancer cells, while in normal cells, neither isolated nor encapsulated EGCG affected cell proliferation, at concentrations <0.15 mg ml(-1). At higher concentrations, both isolated and encapsulated produced similar decreases in proliferation. On the other hand, the bioefficacy on the cancer cell line showed some differences at lower concentrations. The results demonstrated that regardless of the extent of digestion of the nanoencapsulated EGCG, the bioefficacy of EGCG was not diminished, confirming that casein micelles are an appropriate delivery system for polyphenols.


Assuntos
Caseínas/química , Catequina/análogos & derivados , Micelas , Chá/química , Animais , Catequina/química , Catequina/farmacologia , Linhagem Celular , Linhagem Celular Tumoral , Proliferação de Células/efeitos dos fármacos , Camundongos , Polifenóis/química , Polifenóis/farmacologia , Ratos
3.
Food Chem ; 143: 27-32, 2014 Jan 15.
Artigo em Inglês | MEDLINE | ID: mdl-24054208

RESUMO

Many studies have shown that tea catechins bind to milk proteins. This research focused on the association of tea polyphenols with casein micelles, and the consequences of the interactions on the renneting behaviour of skim milk. It was hypothesized that epigallocatechin-gallate (EGCG), the main catechin present in green tea, forms complexes with the casein micelles and that the association modifies the processing functionality of casein micelles. The binding of EGCG to casein micelles was quantified using HPLC. The formation of catechin-casein micelles complexes affected the rennet induced gelation of milk, and the effect was concentration dependent. Both the primary as well as the secondary stage of gelation were affected. These experiments clearly identify the need for a better understanding of the effect of tea polyphenols on the processing functionality of casein micelles, before milk products can be used as an appropriate platform for delivery of bioactive compounds.


Assuntos
Caseínas/química , Catequina/química , Quimosina/metabolismo , Animais , Caseínas/metabolismo , Catequina/metabolismo , Bovinos , Quimosina/química , Digestão , Humanos , Micelas , Leite/química , Leite/metabolismo , Modelos Biológicos , Polifenóis/química , Polifenóis/metabolismo , Ligação Proteica
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