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1.
Int J Food Sci Nutr ; 67(1): 74-82, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-26706903

RESUMO

Bakery products are highly consumed by children and adults and as cereal-derived foods are considered a fundamental part of a balanced diet, but they are usually high in sugar and saturated and trans fat and low in fibre. This study aimed to develop four different bakery products (cookies, croissants, Spanish muffins and Spanish sponge cake) with healthier properties, such as lower fat and sugar content, healthy fatty acid profile and higher fibre content. Margarine and sunflower oil were replaced with high oleic sunflower oil, and inulin was also added. After the modifications, a significant reduction of fat content and kilocalories in all cases, an increment of monounsaturated fat and a decrease in saturated fatty acids in three products were observed. The sensory analysis resulted similar results in both recipes for cookies and lower acceptability in sponge cake, croissants and muffins. Purchase intention only decreased in sponge cake.


Assuntos
Comportamento do Consumidor , Gorduras na Dieta/análise , Grão Comestível , Análise de Alimentos , Manipulação de Alimentos/métodos , Inulina , Ácido Oleico , Adulto , Ingestão de Energia , Ácidos Graxos Monoinsaturados/análise , Humanos , Margarina , Pessoa de Meia-Idade , Odorantes , Óleos de Plantas , Óleo de Girassol , Paladar , Adulto Jovem
2.
J Theor Biol ; 317: 119-25, 2013 Jan 21.
Artigo em Inglês | MEDLINE | ID: mdl-23073471

RESUMO

Serum amyloid A (SAA) is a major acute phase protein in most species, and is widely employed as a health marker. Systemic SAA isoforms (SAA1, and SAA2) are apolipoproteins synthesized by the liver which associate with high density lipoproteins (HDL). Local SAA (SAA3) isoforms are synthesized in other tissues and are present in colostrums, mastitic milk and mammary dry secretions. Of systemic SAA the bulk is monomeric and bound to HDL, and a small proportion is found in serum in a multimeric form with a buried HDL binding site. In most species, systemic SAA could easily be studied by purifying it from serum of diseased individuals by hydrophobic interaction chromatography methods. For years, we were not able to isolate systemic pig SAA using the latter methods, and found that the bulk of pig SAA did not reside in the HDL-rich serum fractions but in the soluble protein fraction mainly as a multimeric protein. Based on these surprising results, we analysed in silico the theoretical properties and predicted the secondary structure of pig SAA by using the published pig primary SAA amino acid sequence. Results of the analysis confirmed that systemic pig SAA had the highest homology with local SAA3 which in other species is the isoform associated with non-hepatic production in tissues such as mammary gland and intestinal epithelium. Furthermore, the primary sequence of the pig SAA N-terminal HDL binding site did differ considerably from SAA1/2. Secondary structure analysis of the predicted alpha-helical structure of this HDL binding site showed a considerable reduction in hydrophobicity compared to SAA1/2. Based on these results, it is argued that systemic acute phase SAA in the pig has the structural properties of locally produced SAA (SAA3). It is proposed that in pig SAA multimers the charged N-terminal sequence is buried, which would explain their different properties. It is concluded that pig systemic SAA is unique compared to other species, which raises questions about the proposed importance of acute phase SAA in HDL metabolism during inflammation in this species.


Assuntos
Proteína Amiloide A Sérica/metabolismo , Sus scrofa/metabolismo , Sequência de Aminoácidos , Animais , Western Blotting , Cromatografia , Sequência Consenso , Eletroforese em Gel de Poliacrilamida , Interações Hidrofóbicas e Hidrofílicas , Lipoproteínas HDL/sangue , Dados de Sequência Molecular , Estrutura Secundária de Proteína , Análise de Sequência de Proteína , Proteína Amiloide A Sérica/química , Proteína Amiloide A Sérica/isolamento & purificação , Sus scrofa/sangue
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