| 1. |
- Alcocer, Marcos, et al.
(författare)
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Ber e 1 protein: the versatile major allergen from Brazil nut seeds.
- 2012
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Ingår i: Biotechnology letters. - Dordrecht : Springer Netherlands. - 0141-5492 .- 1573-6776. ; 34:4, s. 597-610
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Tidskriftsartikel (refereegranskat)abstract
- Due mainly to its extremely high content of sulphur amino acids, Ber e 1 protein, the major allergen from Brazil nut, has attracted much scientific and press attention. Ber e 1 was the main target protein in early biotechnology transgenic work, in early processing studies of plant storage proteins, in plant vacuolar targeting studies and as the main protein in early nutritional supplementation experiments. Ber e 1 was also one of the first food allergens to be unintentionally transferred from one plant to another and was involved in the first reported case of systemic allergic reaction caused by a food allergen transferred in semen. In this review, many of the Ber e 1 unique biotechnological and structural functions are discussed with a particular emphasis on its use as model protein for studies of intrinsic allergenicity of food proteins.
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| 2. |
- Alvarez Fernandez, Marcia, et al.
(författare)
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Enhancement of sulphide production in anaerobic packed bed bench-scale biofilm reactors by sulphate reducing bacteria
- 2006
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Ingår i: Biotechnology Letters. - : Springer Science and Business Media LLC. - 1573-6776 .- 0141-5492. ; 28:3, s. 175-181
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Tidskriftsartikel (refereegranskat)abstract
- Two biofilm reactors, using pumice stone and Poraver as biofilm supports, were run, based on the optimization of sulphide production using a factorial design. The maximum H2S concentrations reached were 10 and 15 mm, respectively, both being appropriate for metal precipitation in effluents. The set-up of the pumice stone biofilm reactor is suitable for application in the mining area in the Bolivian Andean region, where this material is widely available. The use of specific primers for sulphate-reducing bacteria groups permits the identification of the sulphide-producing bacteria present in biofilms.
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| 3. |
- Andersson, Charlotte, et al.
(författare)
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Enhanced Ribosome and tRNA Contents in Escherichia coli Expressing a Truncated Vitreoscilla Hemoglobin Mutant Analyzed by Flow Field-Flow Fractionation
- 2003
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Ingår i: Biotechnology Letters. - 1573-6776. ; 25:18, s. 1499-1504
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Tidskriftsartikel (refereegranskat)abstract
- The ribosome and tRNA levels of Escherichia coli cells, transformed with a native or mutated Vitreoscilla hemoglobin genes (vhb), were investigated using asymmetrical flow field-flow fractionation (AFFFF). Mutagenesis of vhb by error-prone PCR was carried out to alter the growth behavior of microaerobically cultivated native VHb-expressing E. coli. A VHb mutant, pVMT1, was identified, which was able to reach a remarkably high final A600 of 15, the value of which being 160% higher than that of a VHb control carrying pVHb8 (A600 5.8). AFFFF revealed that cells expressing mutant vhbs showed up to a doubling in the number of active 70S ribosomes cell-1, an almost 3-fold increase in the number of tRNAs cell-1, and up to a 26% increase in the mass fraction of active 70S ribosomes.
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| 4. |
- Andersson, Rolf E.
(författare)
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Concentration and partial purification of lipase from Pseudomonas fluorescens
- 1980
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Ingår i: Biotechnology letters. - 0141-5492 .- 1573-6776. ; 2:5, s. 247-252
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Tidskriftsartikel (refereegranskat)abstract
- During ultrafiltration in a hollow fiber device 105 liters of lipase frort Pseudomonas fluorescens was concentrated to 4 liters with a yield of 56% of total initial activity. The concentrated lipase solution was lyophilized and purified on a DEAE-cellulose anion exchanger column. The partly purified lipase was found to probably contain carbohydrates. © 1980 Kluwer Academic Publishers.
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| 5. |
- Andreazza, N, et al.
(författare)
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Production of imidazole alkaloids in cell cultures of jaborandi as affected by the medium pH
- 2009
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Ingår i: Biotechnology letters. - : Springer. - 0141-5492 .- 1573-6776. ; 31:4, s. 607-614
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Tidskriftsartikel (refereegranskat)abstract
- The effect of pH (from 4.8 to 9.8) on the production of pilosine and pilocarpine and on their partition between cell and medium was studied in two lineages (P and PP) of Pilocarpus microphyllus cell suspension cultures. Highest mass accumulation was observed at high pHs and both lineages produced pilocarpine while only lineage PP produced pilosine. Both alkaloids were released in the medium but higher accumulation occurred in the cells. The highest production of pilocarpine was at pH 8.8-9.8 in both cell lineages. Other imidazole alkaloids were also identified in both lineages. At all pHs tested, the pH in the media cultures tended to stabilize around 6 after 10-15 days of cultivation. NO(3) (-) and NH(4) (+) variation in the media might partially explain the pH stabilization.
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| 6. |
- Aragao, Rosa, et al.
(författare)
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Microcultivation of anaerobic bacteria single cells entrapped in alginate microbeads.
- 2013
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Ingår i: Biotechnology Letters. - : Springer Science and Business Media LLC. - 1573-6776 .- 0141-5492. ; 35:3, s. 397-405
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Tidskriftsartikel (refereegranskat)abstract
- Alginate microbeads, produced by emulsion/internal gelation, were studied for the entrapment and microcultivation of microbial cells with biotechnological potential. An anaerobic consortium which was selected for its capacity to degrade complex carbohydrates, and a pure culture of cellulose degrading bacteria were used for entrapment studies. Optimization of conditions for the formation of spherical alginate microbeads in sizes between 20 and 80 μm were examined. The best conditions were achieved by combining rapeseed methyl ester as oil phase and stirring at 100 rpm using a rotation impeller. Calcium alginate microbeads produced under these conditions were shown to present morphological stability, with large pores in the internal matrix that favours microcolony development. Finally, single cells were observed inside the beads after the entrapment procedure and microcolony formation was confirmed after cultivation in cellobiose.
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| 7. |
- Asachi, R., et al.
(författare)
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Fungal autolysate as a nutrient supplement for ethanol and chitosan production by Mucor indicus
- 2011
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Ingår i: Biotechnology letters. - : Springer Netherlands. - 0141-5492 .- 1573-6776. ; 33:12, s. 2405-2409
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Tidskriftsartikel (refereegranskat)abstract
- Mucor indicus can be used to produce ethanol from a variety of sugars, including pentose's. An extract of it, produced by autolysis, could replace yeast extract in culture medium with improved production of ethanol. At 10 g l(-1), the extract gave a higher ethanol yield (0.47 g g(-1)) and productivity (0.71 g l(-1) h(-1)) compared to medium containing yeast extract (yield 0.45 g g(-1); productivity 0.67 g l(-1) h(-1)).
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| 8. |
- Balan, S, et al.
(författare)
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Metal chelate affinity precipitation of RNA and purification of plasmid DNA
- 2003
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Ingår i: Biotechnology Letters. - 1573-6776. ; 25:13, s. 1111-1116
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Tidskriftsartikel (refereegranskat)abstract
- The affinity of metal chelates for amino acids, such as histidine, is widely used in purifying proteins, most notably through six-histidine `tails'. We have found that metal affinity interactions can also be applied to separation of single-stranded nucleic acids through interactions involving exposed purines. Here we describe a metal affinity precipitation method to resolve RNA from linear and plasmid DNA. A copper-charged copolymer of N-isopropyl acrylamide (NIPAM) and vinyl imidazole (VI) is used to purify plasmid from an alkaline lysate of E. coli. The NIPAM units confer reversible solubility on the copolymer while the imidazole chelates metal ions in a manner accessible to interaction with soluble ligands. RNA was separated from the plasmid by precipitation along with the polymer in the presence of 800 mM NaCl. Bound RNA could be recovered by elution with imidazole and separated from copolymer by a second precipitation step. RNA binding showed a strong dependence on temperature and on the type of buffer used.
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| 9. |
- Berglin, Lennart, et al.
(författare)
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In situ generation of iminodiacetic acid groups on nanoporous alumina for the reversible immobilization of enzymes and other biomolecules
- 2014
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Ingår i: Biotechnology letters. - : Springer Science and Business Media LLC. - 0141-5492 .- 1573-6776. ; 36:9, s. 1819-1825
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Tidskriftsartikel (refereegranskat)abstract
- Nanoporous alumina membranes were silanized with aminopropylsilane and iminodiacetic acid (IDA) groups were generated in situ by reaction with iodoacetate. The membranes were mounted in standard filter holders, connected to a HPLC system and saturated with selected metal ions. Cu(II) allowed the capture of chicken muscle lactate dehydrogenase with such stability, repeatability and reproducibility that Michaelis-Menten kinetics could be studied. The IDA surface was stable for months and could be depleted and regenerated with metal ions multiple times without appreciable loss of capacity. The binding of lactate dehydrogenase influenced the backpressure to the extent that could be expected for a monolayer according to Poiseuilles law.
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| 10. |
- Birgisson, Hakon, et al.
(författare)
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A new thermostable alpha-L-arabinofuranosidase from a novel thermophilic bacterium
- 2004
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Ingår i: Biotechnology Letters. - 1573-6776. ; 26:17, s. 1347-1351
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Tidskriftsartikel (refereegranskat)abstract
- An alpha-L-arabinofuranosidase gene was identified in a sequenced genome of a novel thermophilic bacterium, which belongs to the recently described phylum of Thermomicrobia. Amino acid sequence comparison of the enzyme (designated AraF) revealed similarity to glycoside hydrolases of family 51. The gene was cloned into Escherichia coli and its recombinant product expressed and purified. The enzyme appeared to be a hexamer. AraF was optimally active at 70degreesC (over 10 min) and pH 6 having 92% residual activity after 1 h at 70degreesC. AraF had a K-m value of 0.6 rum and V-max value of 122 U mg(-1) on p-nitrophenyl-alpha-L-arabinofuranoside. AraF was almost equally active on branched arabinan and debranched arabinan, properties not previously found in alpha-L-arabinofuranosidases in GH family 51.
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