Effects of Pecan Nut (Carya illinoiensis) and Roselle Flower (Hibiscus sabdariffa) as Antioxidant and Antimicrobial Agents for Sardines (Sardina pilchardus)

The effects of pecan nut (Carya illinoinensis) and roselle flower (Hibiscus sabdariffa) as antioxidant and antimicrobial agents on shelf life extension of sardines (Sardina pilchardus) were evaluated over a period of 5 days at 7 ± 1 °C. Treatments consisted of the addition of 5% and 10% w/w pecan nut, 5% w/w roselle flower and a combination of 5% of each. Physicochemical (lipid oxidation, fatty acids, hexanal and biogenic amines), sensory and microbiological characteristics of fish samples were periodically analyzed. All treatments effectively improved physicochemical quality parameters, with 10% w/w pecan nut having the highest effectiveness. The presence of roselle flower reduced microbial growth. Our findings suggest that addition of a natural preservative combining pecan nut and roselle flower may extend the shelf life of fresh sardines during chilled storage while maintaining quality indexes.Peer ReviewedPostprint (author's final draft

Effects of Pecan Nut (Carya illinoiensis) and Roselle Flower (Hibiscus sabdariffa) as Antioxidant and Antimicrobial Agents for Sardines (Sardina pilchardus)

The effects of pecan nut (Carya illinoinensis) and roselle flower (Hibiscus sabdariffa) as antioxidant and antimicrobial agents on shelf life extension of sardines (Sardina pilchardus) were evaluated over a period of 5 days at 7 ± 1 ºC. Treatments consisted of the addition of 5% and 10% w/w pecan nut, 5% w/w roselle flower and a combination of 5% of each. Physicochemical (lipid oxidation, fatty acids, hexanal and biogenic amines), sensory and microbiological characteristics of fish samples were periodically analyzed. All treatments effectively improved physicochemical quality parameters, with 10% w/w pecan nut having the highest effectiveness. The presence of roselle flower reduced microbial growth. Our findings suggest that addition of a natural preservative combining pecan nut and roselle flower may extend the shelf life of fresh sardines during chilled storage while maintaining quality indexes

Galectins-1, -3 and -9 Are Present in Breast Milk and Have a Role in Early Life Development

Galectins (Gal) are a family of conserved soluble proteins with high affinity for β-galactoside structures. They have been recognized as important proteins for successful pregnancy. However, little is known about their presence in breast milk and their role in early infancy. Gal-1, -3 and -9 concentrations were evaluated by Multiplex immunoassays in mother-infant pairs from the MAMI cohort in maternal plasma (MP) (n = 15) and umbilical cord plasma (UCP) (n = 15) at birth and in breast milk samples (n = 23) at days 7 and 15 postpartum. Data regarding mother and infant characteristics were collected. Gal-9 was present in a lower concentration range than Gal-1 and Gal-3 in plasma, specifically in UCP. A major finding in the current study is that Gal-1, -3 and -9 were detected for the first time in all the transitional breast milk samples and no differences were found when comparing the two breastfeeding time points. Finally, Gal levels were associated with some maternal and infant characteristics, such as gestational age, pregnancy weight gain, maternal diet, the gender, infant growth and infant infections. In conclusion, Gal levels seem to be involved in certain developmental aspects of early life. Keywords: galectin; breast milk; umbilical cord plasma; maternal plasm

Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy

The digestion of gluten generates toxic peptides, among which a highly immunogenic proline-rich 33-mer from wheat α-gliadin, that trigger coeliac disease. Neprosin from the pitcher plant is a reported prolyl endopeptidase. Here, we produce recombinant neprosin and its mutants, and find that full-length neprosin is a zymogen, which is self-activated at gastric pH by the release of an all-β pro-domain via a pH-switch mechanism featuring a lysine plug. The catalytic domain is an atypical 7+8-stranded β-sandwich with an extended active-site cleft containing an unprecedented pair of catalytic glutamates. Neprosin efficiently degrades both gliadin and the 33-mer in vitro under gastric conditions and is reversibly inactivated at pH > 5. Moreover, co-administration of gliadin and the neprosin zymogen at the ratio 500:1 reduces the abundance of the 33-mer in the small intestine of mice by up to 90%. Neprosin therefore founds a family of eukaryotic glutamate endopeptidases that fulfils requisites for a therapeutic glutenase.This study was supported in part by grants from Spanish and Catalan public and private bodies (grant/fellowship references PID2019-107725RG-I00 to F.X.G.-R., A.R.B., U.E. and T.G.; BES-2016-076877 to S.R.M., BES-2015-074583 to L.A.M., Beatriu de Pinós 2018BP00163 to U.E., 2017SGR3 and Fundació La Marató de TV3 201815 to F.X.G.-R., U.E., A.R.B. and T.G.)