Controlled release of molasses melanoidin-like product from hybrid organic-inorganic silica xerogels and its application to the phytoextraction of lead through the Indian mustard.

In this study, we investigate the release of melanoidin-like product (MLP) from hybrid silica xerogels to control the quantity of MLP in the medium for lead phytoextraction. In the preparation of the hybrid organic-inorganic xerogels with MLP, tetraethoxysilane (TEOS), methyltriethoxysilane (MTES), propyltriethoxysilane (PTES), and 3-aminopropyltriethoxysilane (APTES) were used as precursors. The experimental results suggest that the release of MLP can be easily controlled by partially substituting TEOS with the organosilanes.

Simultaneous suppression of magnetic nanoscale powder and fermented bark amendment for arsenic and cadmium uptake by radish sprouts grown in agar medium.

In this study, we effectively suppressed arsenic and cadmium uptake into a plant using magnetic nanoparticle powder (MNP) and fermented bark amendment (FBA) in agar medium. The MNP (which consists of FeO·FeO) quantitatively adsorbed arsenite (As(III)) and the FBA (which mainly consists of bark waste) adsorbed cadmium, regardless of the pH. The properties of MNP and FBA in agar medium were compared based on the amounts of arsenic and cadmium in cultivated radish sprouts.

Bromein, a Bromelain Inhibitor from Pineapple Stem: Structural and Functional Characteristics.

Bromelain inhibitor, "bromein", is a proteinase-inhibitor specific to the cysteine proteinase bromelain from pineapple stem. In the stem, eight bromein isoforms are known to exist, and each isoform has a short peptide (light chain) and a long one (heavy chain) with five disulfide bonds. The three-dimensional structure of the sixth isoform (bromein-6) is composed of inhibitory and stabilizing domains, and each domain contains a three-stranded antiparallel β-sheet.

Molasses melanoidin-like products enhance phytoextraction of lead through three Brassica species.

Previously, it has been suggested that melanoidin-like products (MLP) from sugarcane molasses may accelerate copper phytoextraction. In this study, we evaluated the facilitatory effect of MLP on phytoextraction in a medium including cadmium or lead, the concentrations of which were adjusted around the regulation values of the Soil Contamination Countermeasures Act in Japan. Three Brassica species were tested based on their fast growth, high biomass productivity, and high heavy metal absorption.

Molasses melanoidin promotes copper uptake for radish sprouts: the potential for an accelerator of phytoextraction.

Phytoextraction has been proposed as an alternative remediation technology for heavy metal contamination, and it is well known that chelators may alter the toxicity of heavy metals and the bioavailability in plants. Our previous work demonstrated that an adsorbent-column chromatography can effectively separate melanoidin-like product (MLP) from sugarcane molasses. The aim of this study was to examine the chelating property of MLP and to evaluate the facilitatory influence on the phytoextraction efficiency of Japanese radish.

A secreted protein with plant-specific cysteine-rich motif functions as a mannose-binding lectin that exhibits antifungal activity.

Plants have a variety of mechanisms for defending against plant pathogens and tolerating environmental stresses such as drought and high salinity. Ginkbilobin2 (Gnk2) is a seed storage protein in gymnosperm that possesses antifungal activity and a plant-specific cysteine-rich motif (domain of unknown function26 [DUF26]). The Gnk2-homologous sequence is also observed in an extracellular region of cysteine-rich repeat receptor-like kinases that function in response to biotic and abiotic stresses.

Evaluation of nonionic adsorbent resins for removal of inhibitory compounds from corncob hydrolysate for ethanol fermentation.

The aim of this study was to investigate the effect of XAD4-column treatment on removal of several fermentation inhibitors from corncob hydrolysate (CH). From analysis using a model hydrolysate, more than 99% of 5-hydroxy-methyl furfural, furfural and vanillin were removed by this treatment, and more than 97% of the total xylose, glucose and arabinose remained in the detoxified CH (DCH). The resulting DCH was tested as a substrate for ethanol production by Saccharomyces cerevisiae and Pichia stipitis.

A thermoacidophile-specific protein family, DUF3211, functions as a fatty acid carrier with novel binding mode.

STK_08120 is a member of the thermoacidophile-specific DUF3211 protein family from Sulfolobus tokodaii strain 7. Its molecular function remains obscure, and sequence similarities for obtaining functional remarks are not available. In this study, the crystal structure of STK_08120 was determined at 1.

A study on the self-assembly behavior of dark materials from molasses.

We have previously demonstrated that dark materials (DM) in acidified molasses are effectively adsorbed to Amberlite XAD7HP resin and are eluted from the resin with 0.1 M sodium hydroxide. In this paper, we have characterized the self-assembly behavior of molasses DM by using dynamic and static light scattering in combination with isoelectric focusing and infrared absorption spectroscopy in order to better understand the resin adsorption mechanism.

Novel strategy using an adsorbent-column chromatography for effective ethanol production from sugarcane or sugar beet molasses.

Molasses-based distilleries generate large volumes of a highly polluted and dark brown-colored wastewater. The present work describes the way in which an adsorbent-column chromatography can effectively remove the colorant and produce biomass ethanol from sugarcane or sugar beet molasses. It was found that the color and chemical oxygen demand of the resulting wastewater was respectively reduced by approximately 87% and 28% as compared with conventional molasses fermentation.

Absolute side-chain structure at position 13 is required for the inhibitory activity of bromein.

Bromelain isoinhibitor (bromein), a cysteine proteinase inhibitor from pineapple stem, has a unique double-chain structure. The bromein precursor protein includes three homologous inhibitor domains, each containing an interchain peptide between the light and heavy chains. The interchain peptide in the single-chain precursor is immediately processed by bromelain, a target proteinase.

Proteinase inhibitor from ginkgo seeds is a member of the plant nonspecific lipid transfer protein gene family.

A 9-kD proteinase inhibitor was isolated from the seeds of ginkgo (Ginkgo biloba) and purified to homogeneity. This protein was revealed to partial-noncompetitively inhibit the aspartic acid proteinase pepsin and the cysteine proteinase papain (inhibition constant = 10(-5)-10(-4) m). The cDNA of the inhibitor was revealed to contain a 357-bp open reading frame encoding a 119-amino acid protein with a potential signal peptide (27 residues), indicating that this protein is synthesized as a preprotein and secreted outside the cells.

Separation and characterization of the colored material from sugarcane molasses.

The colored material (X) was effectively separated from sugarcane molasses using reversed-phase chromatography. Characterization of the molecular structure of sample X was performed using infrared absorption (IR) spectrometry, mass spectrometry (MS), and dynamic light scattering (DLS). The IR spectrum was similar to that of commercial humic acid, and the MS analysis showed that the sample possessed relatively small heterogeneous molecules with molecular masses around 234, 446, 657, 868, and 1079 Da.

Crystallization and preliminary X-ray analysis of ginkbilobin-2 from Ginkgo biloba seeds: a novel antifungal protein with homology to the extracellular domain of plant cysteine-rich receptor-like kinases.

The antifungal protein ginkbilobin-2 (Gnk2) from Ginkgo biloba seeds does not show homology to other pathogenesis-related proteins, but does show homology to the extracellular domain of plant cysteine-rich receptor-like kinases. Native Gnk2 purified from ginkgo nuts and the selenomethionine derivative of recombinant Gnk2 (SeMet-rGnk2) were crystallized by the sitting-drop vapour-diffusion method using different precipitants. X-ray diffraction data were collected from Gnk2 at 2.

Purification, characterization, and molecular gene cloning of an antifungal protein from Ginkgo biloba seeds.

A novel basic protein with antifungal activity was isolated from the seeds of Ginkgo biloba and purified to homogeneity. The protein inhibited the growth of some fungi (Fusarium oxysporum, Trichoderma reesei, and Candida albicans) but did not exhibit antibacterial action against Escherichia coli. Furthermore, this protein showed weak inhibitory activity against the aspartic protease pepsin.

Crystallization and preliminary X-ray analysis of the YjgF/YER057c/UK114-family protein ST0811 from Sulfolobus tokodaii strain 7.

ST0811 from Sulfolobus tokodaii strain 7, a member of the YjgF/YER057c/UK114 protein family, was crystallized by the sitting-drop vapour-diffusion method using PEG 10,000 as precipitant. The crystals diffracted X-rays to beyond 2.0 A resolution using an in-house rotating-anode generator.

Purification and characterization of novel proteinase inhibitors from dried figs.

Two types of the natural organic matter P and B were isolated from dried figs by gel permeation and high-performance liquid chromatography. The characterizations of their molecular structures were also performed using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and infrared absorption spectrometry. As a result, these samples were revealed to inhibit the serine and cysteine proteinases chymotrypsin and papain (K(i) = 10(-)(6)-10(-)(4) M).

Characterization of the acidic and basic limbs of a bell-shaped pH profile in the inhibitory activity of bromelain inhibitor VI.

Bromelain inhibitor VI (BI-VI) is a cysteine proteinase inhibitor from pineapple stem and a unique two-chain inhibitor composed of two distinct domains. BI-VI's inhibitory activity toward the target enzyme bromelain is maximal at pH 4 and shows a bell-shaped pH profile with pKa values of about 2.5 and 5.

Susceptibility of the interchain peptide of a bromelain inhibitor precursor to the target proteases bromelain, chymotrypsin, and trypsin.

Bromein, a cysteine proteinase inhibitor from pineapple stem, is a unique double-chain inhibitor. The 27.5-kDa precursor protein is processed by the removal of three interchain, two interdomain, and two terminal-flanking peptides, thus resulting in the release of mature isoinhibitors of approximately 6 kDa.

Determination of the NMR structure of Gln25-ribonuclease T1.

Ribonuclease (RNase) T1 is a guanyloribonuclease, having two isozymes in nature, Gln25- and Lys25-RNase T1. Between these two isozymes, there is no difference in catalytic activity and three-dimensional structure; however, Lys25-RNase T1 is slightly more stable than Gln25-RNase T1. Recently, it has been suggested that the existence of a salt bridge between Lys25 and Asp29/Glu31 in Lys25-RNase T1 contributes to the stability.

Nuclear magnetic resonance studies on the pKa values and interaction of ionizable groups in bromelain inhibitor VI from pineapple stem.

Bromelain inhibitor VI (BI-VI), a cysteine proteinase inhibitor from pineapple stem, is a unique double-chain molecule composed of two distinct domains A and B. In order to clarify the molecular mechanism of the proteinase-inhibitor interaction, we investigated the electrostatic properties of this inhibitor. The inhibitory activity toward bromelain was revealed to be maximal at pH 3-4 and the gross conformation to be stable over a wide range of pH.

Structure-function relationship of bromelain isoinhibitors from pineapple stem.

Bromelain isoinhibitors from pineapple stem (BIs) are unique double-chain inhibitors and inhibit the cysteine proteinase bromelain competitively. The three-dimensional structure was shown to be composed of two distinct domains, each of which is formed by a three-stranded anti-parallel beta-sheet. Unexpectedly, BIs were found to share similar folding and disulfide-bond connectivities not with the cystatin superfamily, but with Bowman-Birk trypsin/chymotrypsin inhibitor (BBI).