Food Bioscienceshttp://hdl.handle.net/11019/62024-03-28T13:17:49Z2024-03-28T13:17:49ZComplete Genome Sequence of the Gamma-Aminobutyric Acid-Producing Strain Streptococcus thermophilus APC151Linares, Daniel M.Arboleya, SilviaRoss, R. PaulStanton, Catherinehttp://hdl.handle.net/11019/36872024-03-01T07:41:53Z2017-04-27T00:00:00ZComplete Genome Sequence of the Gamma-Aminobutyric Acid-Producing Strain Streptococcus thermophilus APC151
Linares, Daniel M.; Arboleya, Silvia; Ross, R. Paul; Stanton, Catherine
Here is presented the whole-genome sequence of Streptococcus thermophilus APC151, isolated from a marine fish. This bacterium produces gamma-aminobutyric
acid (GABA) in high yields and is biotechnologically suitable to produce naturally GABAenriched biofunctional yogurt. Its complete genome comprises 2,097 genes and
1,839,134 nucleotides, with an average GC content of 39.1%.
peer-reviewed
2017-04-27T00:00:00ZSeparation of the effects of denaturation and aggregation on whey-casein protein interactions during the manufacture of a model infant formulaJoyce, Aoife M.Brodkorb, AndréKelly, Alan L.O’Mahony, James A.http://hdl.handle.net/11019/36822024-03-01T07:41:18Z2016-10-10T00:00:00ZSeparation of the effects of denaturation and aggregation on whey-casein protein interactions during the manufacture of a model infant formula
Joyce, Aoife M.; Brodkorb, André; Kelly, Alan L.; O’Mahony, James A.
Denaturation and aggregation of whey protein have been extensively studied but there is limited knowledge of their effects on processing properties of infant milk formulae (IMF) systems. In this study, the separate effects of denaturation and aggregation of whey protein on the physicochemical characteristics during processing of a model IMF were examined. Whey protein solutions (8%, w/w, protein) were pre-heated for 2 min at 72 or 85 °C, followed by addition of 2.2 mM calcium (Ca) (H-BCa), or at 85 °C after addition of the same level of Ca (H-ACa), to give pre-treated whey protein for inclusion in three model IMF systems, encoded as H-72-BCa, H-85-BCa and H-85-ACa, respectively. Unheated control samples without (UH-C) and with (UH-C-Ca) added Ca were also prepared. Model IMF systems (5.2%, w/w, protein, 60:40 whey protein:casein ratio, pH 6.8) were then prepared incorporating these pre-treated whey protein ingredients and subjected to lab-scale high-temperature short-time (HTST) heating at 85 °C for 2 min; whey protein denaturation was >81.2% in all samples after HTST. Aggregation of whey protein resulted in a significantly (P < 0.05) higher viscosity in sample H-85-ACa (8.3 mPa.s) compared to UH-C (4.0 mPa.s), and measurement of Ca ion concentration on heating showed that Ca ions enhanced whey protein aggregation, resulting in larger mean protein particle size. The results also suggest that pre-heating of whey protein had a preventative effect on aggregation of protein during HTST of IMF. This study clearly showed that aggregation is more influential than denaturation in determining viscosity development during HTST treatment of IMF, and that such viscosity development can be controlled by altering protein-protein interactions using, for example, pre-heat treatment of whey protein ingredients.
peer-reviewed
2016-10-10T00:00:00ZForgotten fungi—the gut mycobiome in human health and diseaseHuseyin, Chloe E.O’Toole, Paul W.Cotter, Paul D.Scanlan, Pauline D.http://hdl.handle.net/11019/36802024-03-01T07:42:26Z2017-04-18T00:00:00ZForgotten fungi—the gut mycobiome in human health and disease
Huseyin, Chloe E.; O’Toole, Paul W.; Cotter, Paul D.; Scanlan, Pauline D.
The human body is home to a complex and diverse microbial ecosystem that plays a central role in host health. This includes a diversity of fungal species that is collectively referred to as our ‘mycobiome’. Although research into the mycobiome is still in its infancy, its potential role in human disease is increasingly recognised. Here we review the existing literature available on the human mycobiota with an emphasis on the gut mycobiome, including how fungi interact with the human host and other microbes. In doing so, we provide a comprehensive critique of the methodologies available to research the human mycobiota as well as highlighting the latest research findings from mycological surveys of different groups of interest including infants, obese and inflammatory bowel disease cohorts. This in turn provides new insights and directions for future studies in this burgeoning research area.
peer-reviewed
2017-04-18T00:00:00ZGlycomacropeptide Reduces Intestinal Epithelial Cell Barrier Dysfunction and Adhesion of Entero-Hemorrhagic and Entero-Pathogenic Escherichia coli in VitroFeeney, ShaneRyan, JosephKilcoyne, MichelleJoshi, LokeshHickey, Ritahttp://hdl.handle.net/11019/36752024-03-01T07:42:40Z2017-10-27T00:00:00ZGlycomacropeptide Reduces Intestinal Epithelial Cell Barrier Dysfunction and Adhesion of Entero-Hemorrhagic and Entero-Pathogenic Escherichia coli in Vitro
Feeney, Shane; Ryan, Joseph; Kilcoyne, Michelle; Joshi, Lokesh; Hickey, Rita
In recent years, the potential of glycosylated food components to positively influence health has received considerable attention. Milk is a rich source of biologically active glycoconjugates which are associated with antimicrobial, immunomodulatory, anti-adhesion, anti-inflammatory and prebiotic properties. Glycomacropeptide (GMP) is the C-terminal portion of kappa-casein that is released from whey during cheese-making by the action of chymosin. Many of the biological properties associated with GMP, such as anti-adhesion, have been linked with the carbohydrate portion of the protein. In this study, we investigated the ability of GMP to inhibit the adhesion of a variety of pathogenic Escherichia coli strains to HT-29 and Caco-2 intestinal cell lines, given the importance of E. coli in causing bacterial gastroenteritis. GMP significantly reduced pathogen adhesion, albeit with a high degree of species specificity toward enteropathogenic E. coli (EPEC) strains O125:H32 and O111:H2 and enterohemorrhagic E. coli (EHEC) strain 12900 O157:H7. The anti-adhesive effect resulted from the interaction of GMP with the E. coli cells and was also dependent on GMP concentration. Pre-incubation of intestinal Caco-2 cells with GMP reduced pathogen translocation as represented by a decrease in transepithelial electrical resistance (TEER). Thus, GMP is an effective in-vitro inhibitor of adhesion and epithelial injury caused by E. coli and may have potential as a biofunctional ingredient in foods to improve gastrointestinal health.
peer-reviewed
2017-10-27T00:00:00Z