An isolated cellulolytic from bovine rumen produces ethanol and hydrogen from corn straw.

Background: Lignocellulosic biomass is the most abundant resource on earth. Lignocellulose is mainly composed of cellulose, hemicelluloses, and lignin. The special construction of three kinds of constituents led to the prevention of effective degradation.

[Synthetic biology and rearrangements of microbial genetic material].

As an emerging discipline, synthetic biology has shown great scientific values and application prospects. Although there have been many reviews of various aspects on synthetic biology over the last years, this article, for the first time, attempted to discuss the relationship and difference between microbial genetics and synthetic biology. We summarized the recent development of synthetic biology in rearranging microbial genetic materials, including synthesis, design and reduction of genetic materials, standardization of genetic parts and modularization of genetic circuits.

Isolation and characterization of temperature and alkaline stable bioflocculant from Agrobacterium sp. M-503.

A bacterium isolated from activated sludge of propylene epoxide wastewater was identified as Agrobacterium sp. M-503. It was confirmed to produce bioflocculant with excellent flocculation activity.

Pathway engineering results the altered polyhydroxyalkanoates composition in recombinant Escherichia coli.

To efficiently produce short-chain-length-medium-chain-length polyhydroxyalkanoates copolymer from substrate mixture containing sugars and/or fatty acids, fadA gene mutant was constructed in Escherichia coli DH5α phosphotransferase system (PTS) disrupted strain. Plasmids pCJY02, pBHR68 and pBHR71 were separately introduced into E. coli DH5α (ΔptsG, ΔFadA) by transformation, then the recombinants were cultivated in the medium containing glucose and/or decanoate as carbon resource, respectively.

PEGylation markedly enhances the in vivo potency of recombinant human non-glycosylated erythropoietin: a comparison with glycosylated erythropoietin.

Recombinant human non-glycosylated erythropoietin (rh-ngEpo) expressed in E. coli was attached to polyethylene glycol (PEG) chains with different sizes and structures. The pharmacokinetic properties and in vivo potency of the PEGylated protein were investigated and comparisons were drawn between the conjugates and glycosylated recombinant Epo (rhEpo).

[Construction of the Man8 GlcNAc2 glycosylation Saccharomyces cerevisiae mutant strain].

In Saccharomyces cerevisiae, protein glycosylation passed two different N-linked modification pathways after the export of predominantly Man8 GlcNAc2-containing glycoproteins from ER to the Golgi. The core oligosaccharide undergoes maturation in the Golgi resulting in a Man8-13 GlcNAc2 structure. Alternatively, core structures may be hypermannosylated with up to 200 mannose residues composing of a backbone of alpha1,6-mannosyl residues with branched alpha1, 2- and alpha1,3-mannosyl side chains.

[The product specificity evolution of cyclodextrin glucanotransferase: problems and challenges].

Cyclodextrin glucanotransferase, the essential enzyme for the production of cyclodextrins, has become the focus of scientific research nowadays. Although many related enzyme properties are well known, the crucial factors in product specificity determination remain to be answered. Here, the recent research progresses of cyclodextrin glucanotransferase, especially those about the evolution of product specificity, were reviewed, and the scientific problems were discussed.

[Progress of oligosaccharides biosynthesis in recombinant Escherichia coli].

As more bioactivities of oligosaccharides have been elucidated, researches on biosynthesis of oligosaccharides have drawn more concerns in Glycobiology. A lot of enzymatic methods for the synthesis of oligosacchrides have been developed employing recombinant E. coli expressed glycosyltranferase or synthase of nucleotide-sugar.

Immobilization of UDP-galactose 4-epimerase from Escherichia coli on the yeast cell surface.

UDP-galactose 4-epimerase (EC 5.1.3.

Delivery of nitric oxide released from beta-Gal-NONOate activation by beta-galactosidase and its activity against Escherichia coli.

Beta-galactosyl-pyrrolidinyl diazeniumdiolates (beta-Gal-NONOate) is a new site-specific nitric oxide (NO)-releasing compound, which releases NO once activated by beta-galactosidase. In the present experiment, we used beta-Gal-NONOate as a bactericidal reagent to investigate its effectiveness of NO releasing. Through the evaluation of intracellular NO level and the comparison of survival of E.

[High level expression of PNGase F in Escherichia coli and its bioactivities].

In order to obtain active recombinant PNGase F in Escherichia coli, a prokaryotic expression vector pET28a/PNGase F was constructed. Amplification of PNGase F was obtained using PCR technique employing suitable primers designed according to the PNGase F gene sequence from Flavobacterium nmeningosepticum. The expression of PNGase F gene in LB medium or M9 medium led to the formation of inclusion body and soluble protein, respectively.