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At least 1,063 records · Page 59Linked to original sources
PubMed1995

Purification of human interleukin-2 using the cellulose-binding domain of a prokaryotic cellulase.

Engineering gene fusions which introduce an affinity tag linked to the target polypeptide by a specific protease cleavage site is widely used to facilitate recombinant protein purification. A fusion protein CBDAPT-IL-2, comprised of the cellulose-binding domain (CBD) and Pro-Thr (PT) rich linker of the Cellulomonas fimi endo-beta-1,4-glucanase A (CenA) and a factor Xa cleavage sequence (IleGluGlyArg) fused to the N terminus of human interleukin-2, was produced in Escherichia coli, Streptomyces lividans and mammalian COS cells. CBDAPT-IL-2, secreted from S. lividans or COS cells or recovered from the insoluble fraction of E. coli, could be purified by adsorption on cellulose. The intact fusion protein adsorbed to cellulose was hydrolyzed in situ with factor Xa to release active interleukin-2.

Actinomycetales↗
PubMed1995

[Molecular cloning of cellulase gene from the bacillus].

The CMCase gene from the Bacillus sp. strain E2 was cloned into E. coli DH5 alpha F' using plasmid pBR322 as a vector. Recombinant plasmid pBG3 was isolated from transformants producing CMCase, and the cloned CMCase gene was found to be in a 4.0kb HindIII fragment. The CMCase gene was subcloned in a functional state on a 2.4kb DNA fragment. The optimum pH and temperature for activity of CMCase encoded by pBG3 were pH 6.5 and 55 degrees C respectively. The CMCase could not hydrolyze any natural cellulose examined. Eighty-three percent of the CMCase was detected in the inner cellular fraction, 9% and 8% were in the periplasmic space and medium respectively. Result of Southern hybridization indicates that the cloned DNA fragment was derived from Bacillus sp. strain E2 chromosomal DNA.

Bacillus↗
PubMedDate not supplied

Usefulness of cellulase in recovery of Salmonella spp. from guar gum.

Most foods examined for Salmonella spp. by the procedure described in the U.S. Food and Drug Administration's Bacteriological Analytical Manual are preenriched at a 1:9 sample/broth ratio. However, 25 g guar gum (an emulsifying agent) is not wetted completely in 225 mL of preenrichment broth, and after a 24 h incubation at 35 degrees C, the product is transformed into a viscous, nonpipettable mass. The effects of 4 factors (inorganic salts, pH, temperature, and various enzymes) on the viscosity of the sample/preenrichment mixture during incubation were determined. Addition of various inorganic salts or adjustment of pH from 4.0 to 9.0 had no significant effect on the viscosity of the incubated mixture. Elevated incubation temperatures of 42 degrees, 44 degrees, and 46 degrees C reduced viscosity but were well above the optimal growth temperature for Salmonella, 35 degrees C. Addition of cellulose to lactose broth at a final concentration of 0.01% reduced viscosity of the mixture, making it readily pipettable. At least one Salmonella cell was consistently recovered from 25 g samples of guar gum, which represents a most probable number value of 0.04 cell per g.

Cellulase↗
PubMed1985

Molecular cloning of Erwinia chrysanthemi pectinase and cellulase structural genes.

Erwinia chrysanthemi 3937 secretes four major pectate lyase isoenzymes (PL, EC 4.2.2.2) and one endocellulase (Cx, EC 3.2.1.4). A genomic library of this strain was constructed in the Lambda L47-1 vector, and screened for the presence of PL and Cx on pectate and caboxymethylcellulose agar. Among the seven Cx-positive phage clones, three were shown to encode an enzyme of the same mol. wt. as the one found in the culture supernatant of strain 3937. The 34 PL-positive phage clones were analyzed by electrofocusing and could, according to the PL they produced, be arranged in five classes. Phages from three classes produced three different single PL, named PLb, c and d. No common fragment was evidenced between the inserts of the phages of these three classes. This demonstrated that, in strain 3937, PLb, C, and d were encoded by three different genes called pelB, C, and D. Furthermore, our results suggest the existence of two additional genes encoding PLa and e. In addition, a pectin methylesterase gene was found closely linked to pelD.

Journal Article↗
PubMed1996

News & Notes: Effect of Surfactants on Cellulase Production by Nectria catalinensis

The effect of different nonionic surfactants (Tween 80, Tween 20, Triton X-100) and polyethylene glycol (PEG 6000) was tested on cellulolytic enzyme system production. Tween 80 gave the highest yield of endoglucanase, exoglucanase, and cellobiase at the 20th day of growth, presumably by causing increased permeability of cell membranes and/or by promoting the release of cell-bound enzymes. Maximal yield of endoglucanase was achieved with 1.7 mM Tween 80, whereas exoglucanase and cellobiase were at 0.85 mM. In the same way, this compound increased fungal growth. On the other hand, Tween 20 and Triton X-100 inhibited growth and cellulolytic enzyme production. High yields of endoglucanase and exoglucanase were achieved with PEG 6000 in comparison with the control, presumably by increasing enzyme stability.

Journal Article↗