List of cyanases from plants, fungi and bacteria.

<p>List of cyanases from plants, fungi and bacteria.</p

List of primers used in this study.

<p>List of primers used in this study.</p

Gel filtration and cyanase activities of His-tagged AtCYN, OsCYN and AtCYN mutants (E94L and S117A).

<p>(A) Gel filtration. High Molecular Weight (HMW) Standard: Thyroglobulin, 669 kDa; Ferritin, 440 kDa; Aldolase, 158 kDa; Conalbumin, 75 kDa and Ovalbumin, 43 kDa. And calculated molecular weight: AtCYN, 210.74 kDa; OsCYN, 211.72 kDa; AtCYN-E94L, 71.64 kDa and AtCYN-S117A, 62.76 kDa. (B) Cyanase activities of His-tagged AtCYN, OsCYN and AtCYN mutants (E94L and S117A) at pH 7.7 and 27°C.</p

Decomposition of cyanate by AtCYN and OsCYN <i>in vivo</i>.

<p>Seeds were plated on MS medium containing either 0 mM, 0.5 mM, 1 mM or 2 mM KCNO. Plates were incubated at 4°C for 3 days and then transferred to a growth chamber for 7 days.</p

Coimmunoprecipitation assay demonstrating self-interaction of AtCYN (A) and OsCYN (B).

<p>Although an extremely low amount of OsCYN proteins was detected in the input samples, an identical pattern was shown by OsCYN in the assay. Lane 1: Mock; Lane 2: HA:CYN and FLAG:CYN were detected in the input samples; Lane 3: when anti-HA antibody was added, FLAG:CYN immunoprecipitated with HA:CYN (Lanes 6&8 were controls); Lane 4: when anti-FLAG antibody was added, HA:CYN immunoprecipitated with FLAG:CYN (Lanes 7&9 were controls); Lane 5: Native mouse IgG was used as negative control of antibodies. Bands of HA:CYN and Flag:CYN are indicated with arrows and bands of mouse IgG are indicated with stars.</p

A Fully Biobased Encapsulant Constructed of Soy Protein and Cellulose Nanocrystals for Flexible Electromechanical Sensing

Presently, flexible electromechanical sensors are of particular interest to next generation mobile applications. To enrich the flexible encapsulants, herein, a fully biobased film is developed by cross-linking soy protein isolate (SPI) with nanocross-linker, aldehyde-bearing, cellulose nanocrystals (CNC). Thanks to the enhanced interfacial interaction between SPI and CNC resulting from the Maillard reaction, the protein-rich phase becomes more homogeneous with smaller domain size. Compared with neat SPI film, the resultant composite films exhibit an obviously improved mechanical property and water resistance. In particular, the heat-sealing property of such films is well maintained, which guarantees their application as encapsulation layers to construct flexible electromechanical sensors. These results indicate that green composite films hold promising applications as universal encapsulation materials for integrating flexible movement-monitoring electronics

Influence of pH and temperature on cyanase activity.

<p>The His:AtCYN and His:OsCYN enzymes were purified and their activities assayed <i>in vitro</i>. (A) Effect of pH on cyanase activity at 27°C. BSA was used as a control. (B) Effect of temperature on cyanase activity at pH 7.7.</p

Alignment of catalytic regions of cyanases from fungus, plant and bacterial species.

<p>Accession numbers for each cyanase are listed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0018300#pone-0018300-t001" target="_blank">Table 1</a>. Residues conserved in all sequences are indicated in white type on a black background, the consensus residue or similar residues in all sequences are indicated in white type on a dark grey background and the consensus residue or similar residues in the sequences of cyanases from Dicotyledoneae and Monocotyledoneae are indicated in black type on a light grey background. The predicted catalytic residues in <i>E. coli</i> are indicated above the alignment.</p

Quantitative RT-PCR analysis of <i>AtCYN</i> transcription.

<p>(A) The <i>AtCYN</i> transcript levels in different plant organs. RL (rosette leaves), CL (cauline leaves); (B) and (C) Samples are the 7-day-old seedlings which grew in the MS medium containing KCNO or NaCl. The <i>AtCYN</i> transcript levels in response to treatment with three KCNO concentrations (B) and in response to treatment with 150 mM NaCl (C); (D) The 7-day-old seedlings from the standard MS medium were transferred to the MS medium containing 1 mM KCNO or 150 mM NaCl, and the samples were harvested at different time points. Error bars represent the standard deviation of three biological replicates.</p

Homology modelling of AtCYN and OsCYN.

<p>(A) The predicted structures of AtCYN (blue) and OsCYN (magentas) were similar to the crystal structure of the EcCYN monomer (green). Ball-and-stick figures represent the conserved catalytic residues Arg96, Glu99 (B) and Ser122 of the EcCYN (C). Red dots indicate chloride ions.</p