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Feuk-Lagerstedt, Elisabeth
Alternative names
Publications (9 of 9) Show all publications
Patinvoh, R., Feuk-Lagerstedt, E., Lundin, M., Sárvári Horváth, I. & Taherzadeh, M. J. (2016). Biological pretreatment of chicken feather and biogas production from total broth. Applied Biochemistry and Biotechnology, 180(7), 1401-1415
Open this publication in new window or tab >>Biological pretreatment of chicken feather and biogas production from total broth
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2016 (English)In: Applied Biochemistry and Biotechnology, ISSN 0273-2289, E-ISSN 1559-0291, Vol. 180, no 7, p. 1401-1415Article in journal (Refereed) Published
Keywords
Chicken feather; Pretreatment; Bacillus substilis strain; Keratinase; Biogas production; Mesophilic; Hydrolysate; Total broth; Bacteria granules
National Category
Bioenergy
Identifiers
urn:nbn:se:hb:diva-13563 (URN)10.1007/s12010-016-2175-8 (DOI)000389891800011 ()2-s2.0-84976333954 (Scopus ID)
Available from: 2018-01-17 Created: 2018-01-17 Last updated: 2018-11-28Bibliographically approved
Fellahi, S., Zaghloul, T. I., Feuk-Lagerstedt, E. & Taherzadeh, M. J. (2014). A Bacillus Strain Able to Hydrolyze Alpha- and Beta-Keratin. Journal of Bioprocessing & Biotechniques, 4, 181
Open this publication in new window or tab >>A Bacillus Strain Able to Hydrolyze Alpha- and Beta-Keratin
2014 (English)In: Journal of Bioprocessing & Biotechniques, ISSN 2155-9821, Vol. 4, p. 181-Article in journal (Refereed)
Abstract [en]

The ability to hydrolyze keratin, a rigid and strongly cross-linked protein in the waste of poultry feather and sheep wool, has made keratinase production by microorganisms highly important to the biotechnological industry. A proteindegrading bacterium (C4) was isolated from compost. Based on morphology and biochemical tests, along with 16S rRNA sequencing, the isolated C4 was tentatively identified as Bacillus sp. C4 (2008). The proteolytic activity of the Bacillus sp. C4 strain was broadly specific; it degraded keratinous and non-keratinous proteins to different degrees. Pea pods as substrate generated the highest protease production, followed by soybean meal and sheep wool. Notwithstanding, using wool keratin as a sole source of carbon and nitrogen yielded the highest level of soluble proteins. Furthermore, the C4 bacterium grew well, and produced a significant level of keratinase when using wool and feather as substrates. Supplementing the medium with yeast extract and peptone shortened the time required for feather degradation, but delayed the onset of the wool keratin hydrolysis with two days. The predominant amino acids released in feather hydrolysate were tyrosine, phenylalanine, and histidine. In contrast, the wool lysate was rich in aspartic acid, methionine, tyrosine, phenylalanine, histidine, and lysine. Results established that utilizing the C4 strain for keratin degradation in waste management holds considerable potential.

Place, publisher, year, edition, pages
Omics Publishing Group, 2014
Keywords
Resource Recovery
National Category
Industrial Biotechnology
Research subject
Resource Recovery
Identifiers
urn:nbn:se:hb:diva-1938 (URN)10.4172/2155-9821.1000181 (DOI)2320/14387 (Local ID)2320/14387 (Archive number)2320/14387 (OAI)
Available from: 2015-11-13 Created: 2015-11-13 Last updated: 2016-03-03
Forgács, G., Alinezhad, S., Mirabdollah, A., Feuk-Legerstedt, E. & Sávári Horváth, I. (2011). Biological treatment of chicken feather waste for improved biogas production. Journal of Environmental Sciences(China), 23(10), 1747-1753
Open this publication in new window or tab >>Biological treatment of chicken feather waste for improved biogas production
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2011 (English)In: Journal of Environmental Sciences(China), ISSN 1001-0742, E-ISSN 1878-7320, Vol. 23, no 10, p. 1747-1753Article in journal (Refereed) Published
Abstract [en]

A two-stage system was developed which combines the biological degradation of keratin-rich waste with the production of biogas. Chicken feather waste was treated biologically with a recombinant Bacillus megaterium strain showing keratinase activity prior to biogas production. Chopped, autoclaved chicken feathers (4%, W/V) were completely degraded, resulting in a yellowish fermentation broth with a level of 0.51 mg/mL soluble proteins after 8 days of cultivation of the recombinant strain. During the subsequent anaerobic batch digestion experiments, methane production of 0.35 Nm3/kg dry feathers (i.e., 0.4 Nm3/kg volatile solids of feathers), corresponding to 80% of the theoretical value on proteins, was achieved from the feather hydrolyzates, independently of the pre-hydrolysis time period of 1, 2 or 8 days. Cultivation with a native keratinase producing strain, Bacillus licheniformis resulted in only 0.25 mg/mL soluble proteins in the feather hydrolyzate, which then was digested achieving a maximum accumulated methane production of 0.31 Nm3/kg dry feathers. Feather hydrolyzates treated with the wild type B. megaterium produced 0.21 Nm3 CH4/kg dry feathers as maximum yield.

Place, publisher, year, edition, pages
Elsevier BV, 2011
Keywords
anaerobic digestion, feather waste, keratinase, bacillus licheniformis, bacillus megaterium, gene expression, Energi och material
National Category
Engineering and Technology
Research subject
Resource Recovery
Identifiers
urn:nbn:se:hb:diva-3214 (URN)10.1016/S1001-0742(10)60648-1 (DOI)2320/9733 (Local ID)2320/9733 (Archive number)2320/9733 (OAI)
Available from: 2015-11-13 Created: 2015-11-13 Last updated: 2017-11-19Bibliographically approved
Hashemi Gheinani, A., Haghayegh Jahromi, N., Feuk-Lagerstedt, E. & Taherzadeh, M. J. (2011). RNA silencing of lactate dehydrogenase gene in Rhizopus oryzae. Paper presented at RNAi 2011 Gene Regulation by Small RNAs, 6th International Conference and exhibition, 29-31 March, St Hilda's College, Oxford, UK. Paper presented at RNAi 2011 Gene Regulation by Small RNAs, 6th International Conference and exhibition, 29-31 March, St Hilda's College, Oxford, UK.
Open this publication in new window or tab >>RNA silencing of lactate dehydrogenase gene in Rhizopus oryzae
2011 (English)Conference paper, Poster (with or without abstract) (Other academic)
Keywords
rna interference, direct delivery of sirna, rhizopus oryzae, lactate dehydrogenase, lactic acid, ethanol, Energi och material
National Category
Engineering and Technology Natural Sciences
Research subject
Resource Recovery
Identifiers
urn:nbn:se:hb:diva-6563 (URN)2320/8144 (Local ID)2320/8144 (Archive number)2320/8144 (OAI)
Conference
RNAi 2011 Gene Regulation by Small RNAs, 6th International Conference and exhibition, 29-31 March, St Hilda's College, Oxford, UK
Available from: 2015-12-22 Created: 2015-12-22 Last updated: 2016-03-03
Hashemi Gheinani, A., Haghayegh Jahromi, N., Feuk-Lagerstedt, E. & Taherzadeh, M. J. (2011). RNA silencing of lactate dehydrogenase gene in Rhizopus oryzae. Journal of RNAi and Gene Silencing, 7, 443-448
Open this publication in new window or tab >>RNA silencing of lactate dehydrogenase gene in Rhizopus oryzae
2011 (English)In: Journal of RNAi and Gene Silencing, ISSN 1747-0854, E-ISSN 1747-0854, ISSN 1747-0854, Vol. 7, p. 443-448Article in journal (Refereed) Published
Abstract [en]

Rhizopus oryzae is a filamentous fungus, belonging to the order Mucorales. It can ferment a wide range of carbohydrates hydrolyzed from lignocellulosic materials and even cellobiose to produce ethanol. However, R. oryzae also produces lactic acid as a major metabolite, which reduces the yield of ethanol. In this study, we show that significant reduction of lactic acid production could be achieved by short (25nt) synthetic siRNAs targeting the ldhA gene. The average yield of lactic acid production by R. oryzae during the batch fermentation process, where glucose had been used as a sole carbon source, diminished from 0.07gm/gm in wild type to 0.01gm/gm in silenced samples. In contrast, the average yield of ethanol production increased from 0.39gm/gm in wild type to 0.45gm/gm in silenced samples. These results show 85.7% (gm/gm) reduction in lactic acid production as compared with the wild type R. oryzae, while an increase of 15.4% (gm/gm) in ethanol yield.

Place, publisher, year, edition, pages
Library Publishing Media, 2011
Keywords
delivery, rhizopus oryzae, ldha gene, lactate dehydrogenase, lactic acid, ethanol production, sirna, Energi och material
National Category
Environmental Biotechnology
Identifiers
urn:nbn:se:hb:diva-3138 (URN)2320/8524 (Local ID)2320/8524 (Archive number)2320/8524 (OAI)
Available from: 2015-11-13 Created: 2015-11-13 Last updated: 2017-08-23Bibliographically approved
Feuk-Lagerstedt, E., Mirabdollah, A. & Alinezhad, S. (2010). Optimization of a protoplast transformation method for Bacillus subtilis, Bacillus megaterium, and Bacillus cereus by a plasmid pHIS1525.SplipA. In: Antonio Mendez-Vilas (Ed.), Microorganisms in Industry and Environment. From scientific and industrial research to consumer products. Proceedings of the III International Conference on Environmental, Industrial and Applied Microbiology. Lisbon, Portugal, 2 – 4 December 2009.: (pp. 333-336). World Scientific Publishing Co. Pte. Ltd.
Open this publication in new window or tab >>Optimization of a protoplast transformation method for Bacillus subtilis, Bacillus megaterium, and Bacillus cereus by a plasmid pHIS1525.SplipA
2010 (English)In: Microorganisms in Industry and Environment. From scientific and industrial research to consumer products. Proceedings of the III International Conference on Environmental, Industrial and Applied Microbiology. Lisbon, Portugal, 2 – 4 December 2009. / [ed] Antonio Mendez-Vilas, World Scientific Publishing Co. Pte. Ltd. , 2010, p. 333-336Chapter in book (Other academic)
Place, publisher, year, edition, pages
World Scientific Publishing Co. Pte. Ltd., 2010
Keywords
Energi och material
National Category
Engineering and Technology
Identifiers
urn:nbn:se:hb:diva-4986 (URN)2320/7364 (Local ID)978-981-4322-10-2 (ISBN)2320/7364 (Archive number)2320/7364 (OAI)
Available from: 2015-12-17 Created: 2015-12-17 Last updated: 2018-01-03Bibliographically approved
Alinezhad, S., Mirabdollah, A., Forgács, G., Feuk-Lagerstedt, E. & Sárvári Horváth, I. (2009). Expression of keratinase gene in Bacillus megaterium using an expression vector of pHIS1525.SPlipA and utilization of the resulting recombinant strain for chicken feather degradation prior to biogas production. In: : . Paper presented at BioMicroWorld2009, III International Conference on Environmental, Industrial and Applied Microbiology, 2-4 december, Lissabon, Portugal.
Open this publication in new window or tab >>Expression of keratinase gene in Bacillus megaterium using an expression vector of pHIS1525.SPlipA and utilization of the resulting recombinant strain for chicken feather degradation prior to biogas production
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2009 (English)Conference paper, Poster (with or without abstract) (Other academic)
Abstract [en]

An increasing quantity of chickens is being utilized annually in the poultry industry, producing a huge volume of chicken feather waste which presents a high quality supply of keratin. Keratinases possessing high level of keratinolytic activity on insoluble keratin play a crucial role in hydrolyzing chicken feathers. Ever since the discovery of proteolytic ability as well as water solubility of keratinase, many industrial processes regarding keratinase application have been developed. A recently invented application to handle poultry waste is to utilize feathers for biogas production. Obviously, large amount of keratinase is required to break down the keratin prior to further conversion to biogas. Previously, several researches have shown that certain bacteria are able to produce keratinase but it is still a challenge to find out which bacteria is the most reliable source for the production with high efficiency. These challenges gave rise to the molecular biologists to bring the focus on gene cloning to develop recombinant strains resulting in overproduction of keratinase. Over the course of various cloning and expression experiments of similar proteins, it was found that Bacillus megaterium could be a susceptible host cell for keratinase production. In our study, the keratinase gene from the chromosomal DNA of Bacillus licheniformis ATCC®53757 was PCR amplified and subsequently cloned into Bacillus megaterium expression vector, pHIS1525.SPlipA. Bacillus megaterium ATCC®14945 strain was transformed with the recombinant plasmid, pKERHIS1525.SPlipA. The KER gene was expressed under xylose inducible promoter, and the product was then purified using Ni-NTA affinity chromatography. After 18 h of incubation an extracellular keratinase activity of 29U ml-1 was achieved (one unit of activity was determined as the amount of enzyme required to an increase of 0.01 in A420 after 30 min of incubation at 37°C). The recombinant strain was further examined for feather degradation using intact chicken feather waste as carbon source. The chopped chicken feathers were partially degraded by the recombinant strain after three days of incubation and the total macroscopic digestion was ultimately observed after seven days resulting in a yellowish peptide rich fermentation broth. The biogas potential of the hydrolysate will be compared with that of untreated feathers by performing anaerobic batch digestion experiments.

Keywords
bacillus licheniformis, bacillus megaterium, gene expression, keratinase, feather degradation, biogas production, Energi och material
National Category
Industrial Biotechnology
Identifiers
urn:nbn:se:hb:diva-6323 (URN)2320/5988 (Local ID)2320/5988 (Archive number)2320/5988 (OAI)
Conference
BioMicroWorld2009, III International Conference on Environmental, Industrial and Applied Microbiology, 2-4 december, Lissabon, Portugal
Available from: 2015-12-22 Created: 2015-12-22 Last updated: 2016-11-18Bibliographically approved
Mirabdollah, A., Alinezhad, S., Feuk-Lagerstedt, E. & Sárvári Horváth, I. (2009). Optimization of a protoplast transformation method for Bacillus Subtilis, Bacillus megaterium, and Bacillus Cereus by a plasmid pHIS1525.SplipA. In: : . Paper presented at BioMicroWorld2009, III International Conference on Environmental, Industrial and Applied Microbiology, 2-4 december, Lissabon, Portugal.
Open this publication in new window or tab >>Optimization of a protoplast transformation method for Bacillus Subtilis, Bacillus megaterium, and Bacillus Cereus by a plasmid pHIS1525.SplipA
2009 (English)Conference paper, Poster (with or without abstract) (Other academic)
Abstract [en]

During the past years of gene cloning studies, Escherichia coli has always been a foremost host cell for exogenous genes expressions owing to its high level of protein production and excretion. However, problems relating to low level of extracellular production of some proteins specially the accumulation of cloned proteases within the cells have moved the attentions from E.coli to bacilli bacteria such as B. megaterium, B.subtilis, and B.cereus due to their secretion ability of many different enzymes. Bacillus megaterium is widely used for high-level expression of heterologous proteins with little or no degradation. Bacillus subtilis is a naturally competent host cell for uptake of exogenous DNA, resulting in attractive industrial applications. Bacillus cereus has sporulation capability which makes it suitable for several industrial uses. A conventional approach for transferring DNA into protoplasts or intact cells of bacillus bacteria is chemical transformation, using chemicals through chilling and then shock-heating of the suspension of cells to induce reversible permeabilization of the cell membrane to make it possible for the external DNA to enter into the cells. In most cloning experiments, the transformation with plasmid DNA is performed using Polyethylene glycol (PEG)-induced competence cells. In this study, a PEG-induced protoplast transformation protocol was developed for three different bacillus strains of Bacillus megaterium ATCC®14945, Bacillus Subtilis ATCC®6051, and Bacillus Cereus ATCC®14579. In all cases a plasmid pHIS1525.SPlipA, well working vector in B.megaterium, was applied. Protoplasts were formed in RHAF medium after treating the cells with lysozyme. Two factors, the incubation time and the lysozyme concentration have been found to play the most important role in effective protoplast formation. These two factors were further optimized in this study to elaborate a chemical transformation procedure which can possibly work for other bacillus strains as well. The optical density (A420) and the number of colony-forming units (CFUs) were determined to find the optimal conditions for each strain. The results indicate that PEG-induced protoplast transformation is a sufficient technique when using a plasmid pHIS1525.SPlipA in Bacillus genus.

Keywords
bacillus megaterium, bacillus subtilis, bacillus cereus, peg-induced protoplast transformation, Energi och material
National Category
Other Industrial Biotechnology
Identifiers
urn:nbn:se:hb:diva-6324 (URN)2320/5987 (Local ID)2320/5987 (Archive number)2320/5987 (OAI)
Conference
BioMicroWorld2009, III International Conference on Environmental, Industrial and Applied Microbiology, 2-4 december, Lissabon, Portugal
Available from: 2015-12-22 Created: 2015-12-22 Last updated: 2017-10-05Bibliographically approved
Feuk-Lagerstedt, E., Movitz, C., Pellmé, S., Dahlgren, C. & Karlsson, A. (2007). Lipid raft protecome of the human neutrophil azurophil granule.. Proteomics, 7(2), 194-205
Open this publication in new window or tab >>Lipid raft protecome of the human neutrophil azurophil granule.
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2007 (English)In: Proteomics, ISSN 1615-9853, E-ISSN 1615-9861, Vol. 7, no 2, p. 194-205Article in journal (Refereed) Published
Abstract [en]

Detergent-resistant membrane domains (DRMs) are present in the membranes of azurophil granules in human neutrophils (Feuk-Lagerstedt et al., J. Leukoc. Biol. 2002, 72, 970). Using a proteomic approach, we have now identified 106 proteins in a DRM preparation from these granule membranes. Among these proteins were the lipid raft structural proteins flotillin-1 and -2, cytoskeletal proteins such as actin, vimentin and tubulin, and membrane fusion promoting proteins like annexins and dysferlin. Our results suggest that the azurophil granule membrane, in similarity to the plasma membrane, is an elaborate structure that takes part in intracellular signaling and functions other than the mere delivery of bactericidal effector molecules to the phagosome.

Place, publisher, year, edition, pages
Wiley - VCH Verlag GmbH & Co. KGaA, 2007
Keywords
azurophil granules, detergent resistant membrane domains, lipid rafts, nanolc-ms/ms, Energi och material
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:hb:diva-2356 (URN)10.1002/pmic.200600482 (DOI)2320/3134 (Local ID)2320/3134 (Archive number)2320/3134 (OAI)
Available from: 2015-11-13 Created: 2015-11-13 Last updated: 2018-01-10Bibliographically approved
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