Skip to main content

Impact of feline AIM on the susceptibility of cats to renal disease.

Bacillus thuringiensis is a Gram-positive soil bacterium known as biopesticide bacteria that produce insecticidal proteins called protein crystals (Cry). In the process of insecticides, chitinase advisable to perforate the membrane barrier peritrophic to facilitate the invasion of Cry proteins to the membrane epithelium.

 A chitinase gene from B. thuringiensis successfully expressed in soluble form in Escherichia coli and purified and characterized the gene product. Purified recombinant enzyme, BthChi74, hydrolyzed artificial substrates, 4-nitrophenyl N, N'-diacetyl-β-D-chitobioside [4NP- (GlcNAc) 2], and the natural substrate, colloidal chitin and crystal α-chitin, but  it does not hydrolyze cellulose. BthChi74 shows the catalytic activity under weakly acidic to neutral pH Yeast Recombinant Proteins range at 50 ° C, and it was stable at broad pH range for 24 hours. Differential scanning Uranium (DSF) shows the protein melting temperature (T m) of 63.6 ° C. 

The kinetic analysis revealed k cat and KM values ​​of 1.5 s-1 and 159 pM, respectively, with 4NP- (GlcNAc ) 2 as a substrate. BthChi74 produced (GlcNAc) 2 and GlcNAc of colloidal chitin and α-chitin as substrate, but activity toward both lower than that toward the former. BthChi74 can bind similar to chitin beads, crystal α-chitin and cellulose through a unique family of two carbohydrate binding module (CBM2). BthChi74 structure-function relationship is discussed in relation to other chitinase, such as Listeria chitinase, who has a family of 5 carbohydrate binding module (CBM5).

Impact of feline AIM on the susceptibility of cats to renal disease

Bifunctional recombinant cellulase-xylanase (rBhcell-xyl) from the bacterium Bacillus halodurans polyextremophilic TSLV1 and utility in raising the renewable agro-residues.


The bifunctional CMCase and xylanase genes encoding thermostable (rBhcell-xyl) from Bacillus halodurans TSLV1 has been expressed in Escherichia coli. The resulting recombinant E. coli-xyl rBhcell (CMCase 2272 and 910 U L-1 xylanase). The monomer rBhcell-xyl is ~ 62-kDa protein with temperature and pH optimum of 60 ° C and 6.0 with T1 / 2 7.0 and 3.5 hours at 80 ° C for CMCase and xylanase, respectively. 

The values ​​of apparent K m (CMC and Birchwood xylan) was 3.8 and https://gentaur.cz/ 3.2 mg mL-1. The catalytic efficiency (k cat / K m) values ​​of xylanase and CMCase was 657 mL and 171 mg-1 min-1, respectively. end-product analysis confirms that rBhcell-xyl are endo-acting enzymes unique to exoglucanase activity. 

The rBhcell-xyl a family of enzymes GH5 have catalytic module module and a single carbohydrate binding. RBhcell-xyl action on the cob corn and wheat bran liberated reducing sugars, which can be fermented to bioethanol and fine biochemicals.

Comments

Popular posts from this blog

Kinetic and oligomeric study of Leishmania braziliensis nicotinate/nicotinamide mononucleotide adenylyltransferase.

Nicotinamide adenine dinucleotide (NAD) is an essential coenzyme involved in redox reactions and oxidative stress defense system. Furthermore, the NAD is used as the substrate by a protein that regulates cell f unctions important for DNA repair, Other Recombinant Proteins  genetic and signal transduction, among many others. NAD biosynthesis can be solved through de novo and salvage pathways, which converge at a common step is catalyzed by a nicotinate / nicotinamide mononucleotide adenylyltransferase (NMNAT EC: 2.7.7.1/18).  Here, we report kinetic characterization of NMNAT of Leishmania braziliensis (LbNMNAT), one of the etiologic agent of leishmaniasis, a parasitic disease that is relevant. Expression and purification of recombinant proteins homogeneous 6xHis-LbNMNAT done and kinetic studies, which included analysis of Km, Vmax, kcat and equilibrium constants (KD) for both forward and reverse reactions, is completed. Oligomeric state of the recombinant protein 6xHis-LbNMNAT ...

Effect of recombinant α1-antitrypsin Fc-fused (AAT-Fc)protein on the inhibition of inflammatory cytokine production and streptozotocin-induced diabetes.

α1-Antitrypsin (AAT) is a member of a family of serine proteinase inhibitors which inhibit the activity of serine proteinase enzymes including human neutrophil elastase, cathepsin G and neutrophil proteinase 3. Here, we expr essed recombinant AAT AAT gene Hapten Recombinant Proteins  intact combining to IgG1 constant region to produce soluble recombinant AAT-Fc protein. Recombinant AAT-Fc protein produced in Chinese hamster ovary (CHO) cells and purified using affinity chromatography mini-proteins A.  Recombinant AAT-Fc protein was tested for anti-inflammatory function and AAT-Fc adequately suppressed tumor necrosis factor (TNF) -α-induced interleukin (IL) -6 in human peripheral blood mononuclear cells (PBMC) and inhibit cytokine-induced TNF by different cytokines in mouse Raw 264.7 macrophage cells. However, AAT-Fc failed lipopolysaccharide-induced cytokine production presses in both PBMC and macrophages. In addition, our data indicate that AAT-Fc blocks the development of h...