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Dublin, Ireland

Vanegas C.H.,Institute of Technology Sligo | Hernon A.,Mount Merrion Co. | Bartlett J.,Institute of Technology Sligo
International Journal of Ambient Energy | Year: 2015

Seaweeds are a valuable feedstock in the production of biofuels such as biogas. In order to achieve higher conversion rates, the biomass requires a pretreatment step. However, the use of harsh conditions is detrimental to the environment and negatively affects the biochemical composition of the seaweed, lowering the yields of the products. In this study, Laminaria digitata and Saccharina latissima were pretreated with organic acids and enzymes. The extent of hydrolysis was evaluated by the concentration of reducing sugars (RS) released from the seaweed. Thereafter, the effect of pretreatments on biogas production from L. digitata was investigated in 120 ml batch reactors incubated at 35°C. Oxalic acid and the enzymatic preparation Cellulase (Sigma C9748) improved the recovery of RS. Pretreatments inhibited the anaerobic digestion process and only a 6% increase in biogas production was obtained when the biomass was subjected to a combination of 2.5% citric acid and Cellulase. © 2013, © 2013 Taylor & Francis. Source


Telford J.E.,Mount Merrion Co. | Bones J.,Mount Merrion Co. | McManus C.,Mount Merrion Co. | Saldova R.,Mount Merrion Co. | And 9 more authors.
Journal of Proteome Research | Year: 2012

Atypical antipsychotic drugs, such as olanzapine, have been shown to alleviate the positive, negative and, to a lesser degree, the cognitive symptoms of schizophrenia in many patients. However, the detailed mechanisms of action of these drugs have yet to be elucidated. We have carried out the first investigation aimed at evaluating the effects of olanzapine treatment on the glycosylation of serum proteins in schizophrenia patients. Olanzapine treatment resulted in increased levels of a disialylated biantennary glycan and reduced levels of a number of disialylated bi- and triantennary glycans on whole serum glycoproteins. These changes were not observed on a low-abundance serum protein fraction. α1 acid glycoprotein was identified as a carrier of some of the detected altered oligosaccharides. In addition, glycan analysis of haptoglobin, transferrin, and α1 antitrypsin reported similar findings, although these changes did not reach significance. Exoglycosidase digestion analysis showed that olanzapine treatment increased galactosylation and sialylation of whole serum proteins, suggesting increased activity of specific galactosyltransferases and increased availability of galactose residues for sialylation. Taken together, these findings indicate that olanzapine treatment results in altered glycosylation of serum proteins. © 2012 American Chemical Society. Source

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