The Effect of Rhenium Content on Microstructural Changes and Irradiated Hardening in W-Re Alloy under High-Dose Ion Irradiation.

An amount of 100 dpa Si irradiation was used to study the effect of transmutation rhenium content on irradiated microscopic defects and hardening in W-xRe (x = 0, 1, 3, 5 and 10 wt.%) alloys at 550 °C. The increase in Re content could significantly refine the grain in the W-xRe alloys, and no obvious surface topography change could be found after high-dose irradiation via the scanning electron microscope (SEM).

Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366.

Aspergillus oryzae HML366 is a newly screened cellulase-producing strain. The endoglucanase HML ED1 from A. oryzae HML366 was quickly purified by a two-step method that combines ammonium sulfate precipitation and strong anion exchange column.

Purification and Enzymatic Properties of a Difunctional Glycoside Hydrolase from HML366.

In the study, an extracellular enzyme HML CBH1 was purified from the fermentation solution of HML366, and characterized by biological and molecular analysis. Following the culturing of HML366 under the optimized conditions for enzyme production, an enzyme named HML CBH1 with a molecular weight of 48 kDa was purified using 3000 Da cellulose ultrafiltration column and anion exchange chromatography. The specific activity of the purified enzyme was 9.

One-step purification of two novel thermotolerant β-1,4-glucosidases from a newly isolated strain of Fusarium chlamydosporum HML278 and their characterization.

A newly identified cellulase-producing Fusarium chlamydosporum HML278 was cultivated under solid-state fermentation of sugarcane bagasse, and two new β-glucosides enzymes (BG FH1, BG FH2) were recovered from fermentation solution by modified non-denaturing active gel electrophoresis and gel filtration chromatography. SDS-PAGE analysis showed that the molecular weight of BG FH1 and BG FH2 was 93 kDa and 52 kDa, respectively, and the enzyme activity was 5.6 U/mg and 11.

Identification and characterization of a novel fumarase gene by metagenome expression cloning from marine microorganisms.

Background: Fumarase catalyzes the reversible hydration of fumarate to L-malate and is a key enzyme in the tricarboxylic acid (TCA) cycle and in amino acid metabolism. Fumarase is also used for the industrial production of L-malate from the substrate fumarate. Thermostable and high-activity fumarases from organisms that inhabit extreme environments may have great potential in industry, biotechnology, and basic research.

Biochemical characterization of two novel β-glucosidase genes by metagenome expression cloning.

Two novel β-glucosidase genes designated as bgl1D and bgl1E, which encode 172- and 151-aa peptides, respectively, were cloned by function-based screening of a metagenomic library from uncultured soil microorganisms. Sequence analyses indicated that Bgl1D and Bgl1E exhibited lower similarities with some putative β-glucosidases. Functional characterization through high-performance liquid chromatography demonstrated that purified recombinant Bgl1D and Bgl1E proteins hydrolyzed D-glucosyl-β-(1-4)-D-glucose to glucose.