好アルカリ性Bacillus A-007株のK^+ : 促進ATPaseについて

1.好アルカリ性Bacillus A-007株の生育にとってK^+は必須であった.2.K^+-濃度を制限した培地(1.5mMK^+)で生育させた細胞の膜画分に, K^+により促進されるATPase活性が認められた.3.K^+促進ATPaseは, 動力学的特性及びウワバイン, NaN_3, PCMBに対する感受件において, 同菌株のH^+-ATPaseと明らかに異なっていた.1. K^+ was essential for the growth of an alkalophilic Bacillus A-007. 2. Membrane fraction, which was prepared from the cells grown in K^+ -limited medium (1.5mM K^+), showed K^+ -stimulated ATPase activity. 3. The K^+ -stimulated ATPase was clearly different from H^+ -ATPase on kinetical profile and ouabain-, NaN_3- and PCMB-sensvtivity

MOESM4 of Efficient hydrolysis of raw starch and ethanol fermentation: a novel raw starch-digesting glucoamylase from Penicillium oxalicum

Additional file 4: Figure S3. SDS-PAGE analysis of the rPoGA15A that lacked a SBD and wild-type rPoGA15A. Lane 1, protein molecular weight marker; lane 2, the rPoGA15A lacking SBD; lane 3, the wild-type rPoGA15A

Purification and characterization of a highly efficient calcium-independent α-amylase from Talaromyces pinophilus 1-95

<p>The manuscript was accepted by journal "PLoS ONE" under the title of </p> <p>"Purification and characterization of a highly efficient calcium-independent α-amylase from Talaromyces pinophilus 1-95", with a doi of 10.1371/journal.pone.0121531. The compressed file "submited to Figshare.rar" included five excel files, which were the primary dataset of the table from one to five, respectively.</p

Comparison of enzymatic characteristics among TpAA and previously reported α-amylases.

<p>^aThe enzyme activity was measured using DNS method.</p><p>^bThe enzyme activity was measured using iodine method, thus the result can’t be directly compared with those measured using DNS method.</p><p>NM: Not mentioned in the reference.</p><p>Comparison of enzymatic characteristics among TpAA and previously reported α-amylases.</p

SDS-PAGE and native PAGE analysis of the purified amylolytic enzyme from <i>Talaromyces pinophilus</i> 1–95.

<p>Lane 1: protein molecular weight ladder on SDS-PAGE. Lane 2: the purified amylolytic enzyme from <i>Talaromyces pinophilus</i> 1–95 on SDS-PAGE. Lane 3: the purified amylolytic enzyme from <i>Talaromyces pinophilus</i> 1–95 on native PAGE. Lane 4: zymogram analysis of the purified amylolytic enzyme from <i>Talaromyces pinophilus</i> 1–95 on native PAGE.</p

Substrate specificity of TpAA.

<p>^aData are means ± standard deviation from three replicates. The experiments were repeated three times and similar results were obtained.</p><p>ND: Enzyme activity was undetectable toward this substrate.</p><p>Substrate specificity of TpAA.</p

HPLC analysis of hydrolysates of malto-oligosaccharides produced by the purified amylolytic enzyme from <i>Talaromyces pinophilus</i> 1–95.

<p>The malto-oligosaccharides were hydrolyzed by the purified amylolytic enzyme at 30°C and pH 5.0 for 12 h at an enzyme dose of 0.2 U/mg substrate. The hydrolysates were analyzed by HPLC with a mixture of glucose, maltose (DP2), maltotriose (DP3), maltotetraose (DP4), maltopentaose (DP5), maltohexaose (DP6), and maltoheptaose (DP7) as standards. (A) Mixture of glucose, DP2, DP3, DP4, DP5, DP6, and DP7. (B) The hydrolysate of DP3. (C) The hydrolysate of DP4. (D) The hydrolysate of DP5. (E) The hydrolysate of DP6. (F) The hydrolysate of DP7.</p

Morphological observation of fungal strain 1–95.

<p>Fungal strain 1–95 was cultivated using solid or liquid media, and then the morphological data were collected. (A) The obverse side of fungal strain 1–95. (B) The reverse side of fungal strain 1–95. (C) Fungal strain 1–95 produced red pigment when it was cultured using liquid isolating medium (containing 1% soluble starch). (D) The broom-like conidia generating structure and conidia of fungal strain 1–95.</p

Effects of low-molecular-weight organic solvents on the enzyme activity of TpAA.

<p>^aData are means ± standard deviation from three replicates. The experiments were repeated three times and similar results were obtained.</p><p>Effects of low-molecular-weight organic solvents on the enzyme activity of TpAA.</p

Supplementary Tables from The effect of alkali-soluble lignin on purified core cellulases and hemicellulases activities during hydrolysis of pretreated lignocellulosic biomass

Table S1. Core enzymes activities on different substrates.; Table S2. Statistical model regression coefficients for xylan conversion at three protein mass loadings for EA-CS(-) and EA-CS(+) pretreated biomass.; Table S3. The average difference of glucan conversion and their statistical significance for EA-CS(-) and EA-CS(+) under thirty-one enzyme combinations(at three different enzyme mass loadings, with 7.5, 15, and 30 mg protein/g glucan). Note: sig. here means significance. *: P<0.05; **: P<0.01; ***: P<0.001.; Table S4. The model generated optimum mixture hydrolysis predictions were verified at three total enzyme loadings for both EA-CS(-) and EA-CS(+)