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1.
Bioresour Technol ; 289: 121682, 2019 Oct.
Article in English | MEDLINE | ID: mdl-31271918

ABSTRACT

Microalgal biomass is considered as the most promising feedstock for sustainable production of liquid fuels. Lipid production with Microchloropsis salina was studied in open thin-layer cascade (TLC) photobioreactors with a surface area of 8 m2 applying a physically simulated Mediterranean summer climate. High lipid concentrations of up to 6.6 g L-1 with 46% (w w-1) total lipids in dry cell mass were achieved in two-phase batch processes applying a nitrogen limitation. The two-phase batch process was transferred into a continuously operated reactor cascade of two TLC photobioreactors. Microchloropsis salina cells were produced continuously in the first photobioreactor, whereas continuous lipid production was enabled in the second, nitrogen-limited TLC photobioreactor resulting in continuous production of 3.0 g L-1 lipids with a high overall lipid space-time-yield of 0.2 g L-1 d-1. The control of alkalinity to about 10 mM resulted in high CO2 conversion efficiencies of 84-87%.


Subject(s)
Lipids/biosynthesis , Microalgae/metabolism , Biomass , Nitrogen/metabolism , Photobioreactors
2.
Appl Microbiol Biotechnol ; 100(3): 1077-1088, 2016 Feb.
Article in English | MEDLINE | ID: mdl-26590582

ABSTRACT

The quality and regulation of the incident light is crucial in microalgae cultivation processes. Depending on wavelength, spectrum, and intensity, growth characteristics and biochemical composition of these organisms vary. With mainly fluorescent lamps (FL) used previously for illumination, such variabilities could not be studied adequately due to their broad emission spectrum. In contrast, light-emitting diodes (LEDs) emit a very narrow wavelength band and enable flexible photobioreactor designs due to their small size. This review provides a condensed overview on the application of LEDs in microalgal cultivation processes. It summarizes the current availability and applicability of LED technologies as an illumination source for research-focused photobioreactor systems. A particular focus is the use of narrow-wavelength LEDs to address fundamental as well as applied aspects of light color on algae biomass and value-added compound formation. In this respect, the application of internal and external illumination systems is reviewed together with trends in the industrial use of LED systems to intensify algae process efficiency.


Subject(s)
Biotechnology/instrumentation , Biotechnology/trends , Microalgae/growth & development , Microalgae/radiation effects , Biomass , Biotechnology/methods , Light , Photobioreactors
3.
Neurodegener Dis ; 5(3-4): 232-6, 2008.
Article in English | MEDLINE | ID: mdl-18322399

ABSTRACT

BACKGROUND: In Alzheimer's disease (AD), brain butyrylcholinesterase (BChE) co-localizes with beta-amyloid (Abeta) fibrils. AIMS: In vitro testing of the significance of this phenomenon to AD progress. METHODS: A thioflavine T (ThT) fluorogenic assay, photo-induced cross-linking and quantifiable electron microscopy served to compare the effect on Abeta fibril formation induced by highly purified recombinant human BChE (rBChE) produced in the milk of transgenic goats with that of serum-derived human BChE. RESULTS: Both proteins at 1:50 and 1:25 ratios to Abeta dose-dependently prolonged the ThT lag time and reduced the apparent rate of Abeta fibril formation compared to Abeta alone. Photo-induced cross-linking tests showed that rBChE prolonged the persistence of amyloid dimers, trimers and tetramers in solution, whereas Abeta alone facilitated precipitation of such multimers from solution. Transmission electron microscopy showed that rBChE at 1:100 to Abeta prevented the formation of larger, over 150-nm-long, Abeta fibrils and reduced fibril branching compared to Abeta alone as quantified by macro programming of Image Pro Plus software. CONCLUSION: Our findings demonstrate that rBChE interacts with Abeta fibrils and can attenuate their formation, extension and branching, suggesting further tests of rBChE, with unlimited supply and no associated health risks, as a therapeutic agent for delaying the formation of amyloid toxic oligomers in AD patients.


Subject(s)
Amyloid beta-Peptides/antagonists & inhibitors , Amyloid beta-Peptides/metabolism , Amyloid/metabolism , Butyrylcholinesterase/metabolism , Milk/enzymology , Recombinant Proteins/metabolism , Amyloid/genetics , Amyloid beta-Peptides/genetics , Animals , Animals, Genetically Modified , Butyrylcholinesterase/genetics , Butyrylcholinesterase/isolation & purification , Butyrylcholinesterase/physiology , Female , Goats , Humans , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics
4.
Eur J Biochem ; 268(11): 3214-22, 2001 Jun.
Article in English | MEDLINE | ID: mdl-11389723

ABSTRACT

The reactions of lactoperoxidase (LPO) intermediates compound I, compound II and compound III, with nitrite (NO2(-)) were investigated. Reduction of compound I by NO2(-) was rapid (k2 = 2.3 x 10(7) M(-1) x s(-1); pH = 7.2) and compound II was not an intermediate, indicating that NO2* radicals are not produced when NO2(-) reacts with compound I. The second-order rate constant for the reaction of compound II with NO2(-) at pH = 7.2 was 3.5 x 10(5) M(-1) x s(-1). The reaction of compound III with NO2(-) exhibited saturation behaviour when the observed pseudo first-order rate constants were plotted against NO2(-) concentrations and could be quantitatively explained by the formation of a 1 : 1 ratio compound III/NO2(-) complex. The Km of compound III for NO2(-) was 1.7 x 10(-4) M and the first-order decay constant of the compound III/ NO2(-) complex was 12.5 +/- 0.6 s(-1). The second-order rate constant for the reaction of the complex with NO2(-) was 3.3 x 10(3) M(-1) x s(-1). Rate enhancement by NO2(-) does not require NO2* as a redox intermediate. NO2(-) accelerates the overall rate of catalysis by reducing compound II to the ferric state. With increasing levels of H2O2, there is an increased tendency for the catalytically dead-end intermediate compound III to form. Under these conditions, the 'rescue' reaction of NO2(-) with compound III to form compound II will maintain the peroxidatic cycle of the enzyme.


Subject(s)
Lactoperoxidase/chemistry , Nitrites/pharmacology , Benzothiazoles , Catalysis/drug effects , Dose-Response Relationship, Drug , Hydrogen Peroxide/chemistry , Kinetics , Oxidation-Reduction , Spectrophotometry , Sulfonic Acids/chemistry
5.
J Colo Dent Assoc ; 49(4): 14-6, 1971 May.
Article in English | MEDLINE | ID: mdl-5282054
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