Sheffield, United Kingdom
Sheffield, United Kingdom

Time filter

Source Type

Hamed S.M.,Water and Environment Institute | Raut M.P.,ChELSI Institute | Jaffe S.R.P.,ChELSI Institute | Wright P.C.,Northumbria University
International Journal of Hydrogen Energy | Year: 2017

In this study, we tested four algal species (Synechocystis sp. PCC 6803 and three novel algal species isolated from Egyptian paddy rice soil, having high 16S rRNA gene sequence identity to Nostoc spongiaeforme, Parachlorella kessleri SAG 211-11 and Nostoc sp. PCC 7524) under aerobic, anaerobic and 3% CO2-supplemented anaerobic condition. Significant changes in photohydrogen production, morphology, chlorophyll a and protein content/pattern were observed in all species, when grown in these different conditions. H2 production was higher in anaerobic condition in all species with the highest H2 production rate of 4 mmol H2 mg Chla -1 h-1 at 24 h in Synechocystis sp. In contrast, Chla content and protein content decreased (%) in N. spongiaeforme, (29%, 58%), P. kessleri (47%, 7%) and Nostoc sp. (59%, 65%).The anaerobic condition with 3% CO2 stimulated early production of H2 in all species except Synechocystis sp. Our results compared all selected algal species under different growth conditions for the screening of a superior H2-producing algal species that can help to address engineering challenges in the field of large-scale H2 photoproduction by microalgae. © 2017 Hydrogen Energy Publications LLC.


Pewsey E.,University of Sheffield | Bruce C.,University of Sheffield | Tonge P.,University of Sheffield | Evans C.,ChELSI Institute | And 5 more authors.
Journal of Proteome Research | Year: 2010

The use of stem cells for generating cell types suitable for therapy is dependent on understanding the mechanisms, and identifying biomarkers, that control cell fate into different lineages. In this study, we aimed to characterize the nuclear protein dynamics of NTERA-2 cells undergoing retinoic acid-induced differentiation. We focused specifically on the first six days of differentiation, to provide insight into the earliest differentiation events, and employed techniques to specifically monitor the nuclear proteome. Well-characterized gene expression markers were used to precisely stage cell differentiation across the experimental time course. A combination of the novel iTRAQ and ExacTag labeling technologies, together with LC-ESI tandem mass spectrometry, were then used to accurately measure nuclear protein expression changes occurring within these differentiation-staged cells. We report proteins that showed significantly altered expression over the first 6 days of differentiation. Extensive bioinformatic analysis was undertaken, resulting in the construction of a novel interactome network, which revealed the temporal dynamics of the nuclear protein network in the context of neuronal differentiation. © 2010 American Chemical Society.


Jaffe S.R.P.,ChELSI Institute | Strutton B.,ChELSI Institute | Levarski Z.,Comenius University | Pandhal J.,ChELSI Institute | Wright P.C.,ChELSI Institute
Current Opinion in Biotechnology | Year: 2014

Chinese Hamster Ovary cells are the most popular host expression system for the large-scale production of human therapeutic glycoproteins, but, the race to engineer Escherichia coli to perform glycosylation is gathering pace. The successful functional transfer of an N-glycosylation pathway from Campylobacter jejuni to Escherichia coli in 2002 can be considered as the crucial first engineering step. Here, we discuss the recent advancements in the field of N-glycosylation of recombinant therapeutic proteins in E. coli cells, from the manipulation of glycan composition, to the improvement in glycosylation efficiency, along with the challenges that remain before E. coli can be available as an industry host cell for economically viable glycoprotein production. © 2014 Elsevier Ltd.


Deines P.,ChELSI Institute | Deines P.,University of Sheffield | Deines P.,University of Auckland | Sekar R.,ChELSI Institute | And 5 more authors.
Applied Microbiology and Biotechnology | Year: 2010

This study presents a new coupon sampling device that can be inserted directly into the pipes within water distribution systems (WDS), maintaining representative near wall pipe flow conditions and enabling simultaneous microscopy and DNA-based analysis of biofilms formed in situ. To evaluate this sampling device, fluorescent in situ hybridization (FISH) and denaturing gradient gel electrophoresis (DGGE) analyses were used to investigate changes in biofilms on replicate coupons within a non-sterile pilot-scale WDS. FISH analysis demonstrated increases in bacterial biofilm coverage of the coupon surface over time, while the DGGE analysis showed the development of increasingly complex biofilm communities, with time-specific clustering of these communities. This coupon design offers improvements over existing biofilm sampling devices in that it enables simultaneous quantitative and qualitative compositional characterization of biofilm assemblages formed within a WDS, while importantly maintaining fully representative near wall pipe flow conditions. Hence, it provides a practical approach that can be used to capture the interactions between biofilm formation and changing abiotic conditions, boundary shear stress, and turbulent driven exchange within WDS. © Springer-Verlag 2010.


PubMed | Comenius University and ChELSI Institute
Type: | Journal: Current opinion in biotechnology | Year: 2014

Chinese Hamster Ovary cells are the most popular host expression system for the large-scale production of human therapeutic glycoproteins, but, the race to engineer Escherichia coli to perform glycosylation is gathering pace. The successful functional transfer of an N-glycosylation pathway from Campylobacter jejuni to Escherichia coli in 2002 can be considered as the crucial first engineering step. Here, we discuss the recent advancements in the field of N-glycosylation of recombinant therapeutic proteins in E. coli cells, from the manipulation of glycan composition, to the improvement in glycosylation efficiency, along with the challenges that remain before E. coli can be available as an industry host cell for economically viable glycoprotein production.

Loading ChELSI Institute collaborators
Loading ChELSI Institute collaborators