Konferencija Što činimo po pitanju transparentnosti

Additional file 2: Figure S2. PCR and phenotypic analysis of the Δcre1 strain T. reesei SDC11. a PCR analysis of T. reesei SDC11 with SP4 as control. 1 and 2 represent the fragment (upstream region and open reading frame of gene cre1) amplificated by the prime pair cre1-2426UF/cre1-1069R in T. reesei SDC11 and SP4, respectively; 3 and 4 represent the internal fragment of gene cre1 amplificated by the prime pair cre1-497F/cre1-1069R in T. reesei SDC11 and SP4, respectively. 5 and 6 represent the fragment of gene pyrG amplificated by the prime pair pyrG-UF1/pyrG-2426DR in T. reesei SDC11 and SCP11, respectively. b Southern blot analysis of the genomic DNA isolated from SP4 and SCP11, which were digested with EcoRI/HindIII. A 5.5-kb fragment is present in the parental strain SP4, and a 7.0-kb band is shown in Δcre1 + pyrG strain SCP11. c Growth of T. reesei SN1, Δcre1 + pyrG strain SCP11 and Δcre1 strain SDC11 on MM plate. d Growth of T. reesei SP4, Δcre1 + pyrG strain SCP11 and Δcre1 strain SDC11 on the MM plate containing uracil (0.1%)

Concentration of ethanol and glucose obtained with and without fermentation medium.

<p>Other S-SSF conditions were cellulase loading of 50 FPU/g oven-dried solid residues, substrate concentration of 8.5%, pre-hydrolysis temperature of 50°C, pre-hydrolysis time of 12 h, pH 4.8, and fermentation temperature of 36°C.</p

Optimum (A) temperature and (B) pH and (C) thermal and (D) pH stability of PelC.

<p>(E) Substrate specificity of PelC.</p

Effect of pre-hydrolysis time onconcentration of ethanol and glucose in S-SSF of pretreated corn stover with LHW.

<p>S-SSF conditions are same as that in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0095455#pone-0095455-g001" target="_blank">Figure 1</a> except pre-hydrolysis time.</p

Oligonucleotide primers used for the construction of plasmids.

<p>Primers were used during PCR to generate various DNA fragments.</p

Effect of fermentation temperature on concentration of ethanol and glucose in S-SSF of pretreated corn stover with LHW.

<p>S-SSF conditions are same as that in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0095455#pone-0095455-g001" target="_blank">Figure 1</a> except fermentation temperature.</p

Changes in surface area, pore volume and pore diameter of corn stover before and after LHW pretreatment.

<p>Changes in surface area, pore volume and pore diameter of corn stover before and after LHW pretreatment.</p

SEM micrographs of untreated and LHW-pretreated corn stover.

<p>a: untreated corn stover; b: pretreated corn stover at severity factor of 3.95; c: pretreated at severity factor of 4.54.</p

Chemical compositions of the prehydrolysates and solid residues obtained from LHW pretreatment of corn stover.

<p>*Based on all of xylose and xylan in prehydrolysate.</p><p>**Based on oven dry weight of solid residue, except yield that on basis of weight of untreated corn stover.</p

A Bioelectrochemical Method for the Quantitative Description of the Hofmeister Effect of Ionic Liquids in Aqueous Solution

It is imperative to establish a simple, efficient, and practical method to investigate the Hofmeister effect of ionic liquids (ILs) on the behavior of proteins (enzymes). In this study, the effects of the cations and anions of different ILs in aqueous media on the structural stability of horseradish peroxidase (HRP), a model oxidoreductase, were systematically investigated using electrochemical methods. It is found that without ILs no direct electron transfer current signals of HRP appear at bare glassy carbon electrode (GCE) in phosphate buffer (pH 7.0) even after incubation and accumulation at a negative potential. In the presence of ILs, however, a current signal occurs at GCE, depending on the structure of the IL and its concentration. A linear relationship between the peak currents and the scan rates demonstrates that the direct electron transfer is a surface-confined thin-layer electrochemical process. The redox signal at GCE is from the heme of HRP. An IL has a perturbing effect on the HRP structure. The anodic peak current of HRP at GCE, the catalytic activity of HRP, and the secondary structure of HRP are well correlated. Different cations or anions at varied concentrations have different effects on the structural stability of HRP, resulting in different current signals at GCE. Thus, the anodic peak current of HRP at GCE can be used as an indicator to quantitatively characterize the effect of ILs on the structural stability of HRP. The present Hofmeister series for cations and anions is in good agreement with that reported elsewhere. To our knowledge, this is a first attempt to establish a simple and practical electrochemical method to correlate Hofmeister effects with characteristics of ions and solvents. The present investigation not only deepens our understanding of the complex electrochemical behavior of proteins in ILs media but also offers a practical guidance to designing “green” and biocompatible ILs for protein (enzyme) separation, purification, and enzymatic catalysis and conversion