Complete Genome Sequence of Elizabethkingia sp. BM10, a Symbiotic Bacterium of the Wood-Feeding Termite Reticulitermes speratus KMT1.

Elizabethkingia sp. BM10 was isolated from the hindgut of the wood-feeding termite Reticulitermes speratus KMT1. It had cellobiohydrolase and β-glucosidase activities but not endo-β-glucanase activity.

Sanitizing Effect of Ethanol Against Biofilms Formed by Three Gram-Negative Pathogenic Bacteria.

Sanitizing effect of ethanol on a Yersinia enterocolitica biofilm was evaluated in terms of biomass removal and bactericidal activity. We found that 40 % ethanol was most effective for biofilm biomass removal; however, no significant difference was observed in bactericidal activity between treatment with 40 and 70 % ethanol. This unexpected low ethanol concentration requirement for biomass removal was confirmed using biofilms of two additional pathogenic bacteria, Aeromonas hydrophila and Xanthomonas oryzae.

Rapid saccharification for production of cellulosic biofuels.

The economical production of biofuels is hindered by the recalcitrance of lignocellulose to processing, causing high consumption of processing enzymes and impeding hydrolysis of pretreated lignocellulosic biomass. We determined the major rate-limiting factor in the hydrolysis of popping pre-treated rice straw (PPRS) by examining cellulase adsorption to lignin and cellulose, amorphogenesis of PPRS, and re-hydrolysis. Based on the results, equivalence between enzyme loading and the open structural area of cellulose was required to significantly increase productive adsorption of cellulase and to accelerate enzymatic saccharification of PPRS.

Purification and characterization of a thermostable cellobiohydrolase from Fomitopsis pinicola.

A screening for cellobiohydrolase (CBH) activity was performed and Fomitopsis pinicola KMJ812 was selected for further characterization as it produced a high level of CBH activity. An extracellular CBH was purified to homogeneity by sequential chromatography of F. pinicola culture supernatants.

One-step purification and characterization of a beta-1,4-glucosidase from a newly isolated strain of Stereum hirsutum.

A highly efficient beta-1,4-glucosidase (BGL) secreting strain, Stereum hirsutum SKU512, was isolated and identified based on morphological features and sequence analysis of internal transcribed spacer rDNA. A BGL containing a carbohydrate moiety was purified to homogeneity from S. hirsutum culture supernatants using only a single chromatography step on a gel filtration column.

Symbiotic adaptation of bacteria in the gut of Reticulitermes speratus: low endo-beta-1,4-glucanase activity.

The termite is a good model of symbiosis between microbes and hosts and possesses an effective cellulose digestive system. Oxygen-tolerant bacteria, such as Dyella sp., Chryseobacterium sp.

Purification and characterization of a thermostable beta-1,3-1,4-glucanase from Laetiporus sulphureus var. miniatus.

A beta-1,3-1,4-glucanase from the fungus Laetiporus sulphureus var. miniatus was purified as a single 26 kDa band by ammonium sulfate precipitation, HiTrap Q HP, and UNO Q ion-exchange chromatography, with a specific activity of 29 U/mg. The molecular mass of the native enzyme was 52 kDa as a dimer by gel filtration.

Characterization of a recombinant beta-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus.

A recombinant beta-glucosidase from Caldicellulosiruptor saccharolyticus DSM 8903 with a specific activity of 13 U/mg was purified by heat treatment and His-Trap affinity chromatography and identified as a single 54 kDa band on SDS-PAGE. The molecular mass of the native enzyme was 108 kDa as a dimer by gel filtration. beta-Glucosidase showed optimum activity at pH 5.

Characterization of endo-beta-1,4-glucanase from a novel strain of Penicillium pinophilum KMJ601.

A novel endo-beta-1,4-glucanase (EG)-producing strain was isolated and identified as Penicillium pinophilum KMJ601 based on its morphology and internal transcribed spacer (ITS) rDNA gene sequence. When rice straw and corn steep powder were used as carbon and nitrogen sources, respectively, the maximal EG activity of 5.0 U mg protein(-1), one of the highest levels among EG-producing microorganisms, was observed.

Purification and characterization of a beta-1,4-glucosidase from a newly isolated strain of Fomitopsis pinicola.

An efficient beta-1,4-glucosidase (BGL) producing strain, Fomitopsis pinicola KMJ812, was isolated and identified based on morphological features and sequence analysis of internal transcribed spacer rDNA. An extracellular BGL was purified to homogeneity by sequential chromatography of F. pinicola culture supernatants on a DEAE-sepharose column, a gel filtration column, and then on a Mono Q column with fast protein liquid chromatography.

Degradation of cellulose by the major endoglucanase produced from the brown-rot fungus Fomitopsis pinicola.

An endoglucanase that is able to degrade both crystalline and amorphous cellulose was purified from the culture filtrates of the brown-rot fungus Fomitopsis pinicola grown on cellulose. An apparent molecular weight of the purified enzyme was approximately 32 kDa by SDS-PAGE analysis. The enzyme was purified 11-fold with a specific activity of 944 U/mg protein against CMC.

Functional analysis of a gene encoding endoglucanase that belongs to glycosyl hydrolase family 12 from the brown-rot basidiomycete Fomitopsis palustris.

The brown-rot basidiomycete Fomitopsis palustris is known to degrade crystalline cellulose (Avicel) and produce three major cellulases, exoglucanases, endoglucanases, and beta- glucosidases. A gene encoding endoglucanase, designated as cel12, was cloned from total RNA prepared from F. palustris grown at the expense of Avicel.

The brown-rot basidiomycete Fomitopsis palustris has the endo-glucanases capable of degrading microcrystalline cellulose.

Two endoglucanases with processive cellulase activities, produced from Fomitopsis palustris grown on 2% microcrystalline cellulose (Avicel), were purified to homogeneity by anion-exchange and gel filtration column chromatography systems. SDS-PAGE analysis indicated that the molecular masses of the purified enzymes were 47 kDa and 35 kDa, respectively. The amino acid sequence analysis of the 47-kDa protein (EG47) showed a sequence similarity with fungal glycoside hydrolase family 5 endoglucanase from the white-rot fungus Phanerochaete chrysosporium.

Prediction of glass transition temperature (T(g)) of some compounds in organic electroluminescent devices with their molecular properties.

We have studied the quantitative structure-property relationship between descriptors representing the molecular structure and glass transition temperature (T(g)) for 103 molecules including organic electroluminescent (EL) devices materials. Eighty-six descriptors were introduced and among them seven descriptors (one topological descriptor, one thermodynamic descriptor, one spatial descriptor, one structural descriptor, and three electrostatic descriptors) were selected by Genetic Algorithm (GA). The 81 molecules chosen randomly among 103 compounds were used as a training set, and the remaining 22 molecules were used as a prediction set.