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Endoglucanase Activity (endoglucanase + activity)
Selected AbstractsIsolation and identification of mixed linked , -glucan degrading bacteria in the intestine of broiler chickens and partial characterization of respective 1,3-1,4- , -glucanase activitiesJOURNAL OF BASIC MICROBIOLOGY, Issue 3 2006Lutz Beckmann Media with 1,3-1,4- , -glucans as selective markers were used for isolation of non-starch-polysaccharide (NSP) degrading bacteria from the intestinal tract of broiler chicken. Formerly unknown 1,3-1,4- , endoglucanase activities in various bacterial species were identified in this study. E. faecium , Streptococcus , Bacteroides and Clostridium strains seem to be responsible for degradation of mixed linked , -glucans in the small intestine and in the hind gut of chickens. Strict anaerobic bacteria (Bacteroides ovatus , B. uniformis , presumably B. capillosus and Clostridium perfringens ) as well as an unidentified bacterium with 98% 16S rDNA homology to an uncultered chicken cecum bacterium were isolated. Additionally, Streptococcus bovis with 1,3-1,4- , -endoglucanase activity was also detected. Different 1,3-1,4- , -endoglucanase activity profiles were observed in SDS/PAGE zymograms. (© 2006 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Purification, characterization and amino-acid sequence analysis of a thermostable, low molecular mass endo-,-1,4-glucanase from blue mussel, Mytilus edulisFEBS JOURNAL, Issue 16 2000Bingze Xu A cellulase (endo-,-1,4- d -glucanase, EC 3.2.1.4) from blue mussel (Mytilus edulis) was purified to homogeneity using a combination of acid precipitation, heat precipitation, immobilized metal ion affinity chromatography, size-exclusion chromatography and ion-exchange chromatography. Purity was analyzed by SDS/PAGE, IEF and RP-HPLC. The cellulase (endoglucanase) was characterized with regard to enzymatic properties, isoelectric point, molecular mass and amino-acid sequence. It is a single polypeptide chain of 181 amino acids cross-linked with six disulfide bridges. Its molecular mass, as measured by MALDI-MS, is 19 702 Da; a value of 19 710.57 Da was calculated from amino-acid composition. The isoelectric point of the enzyme was estimated by isoelectric focusing in a polyacrylamide gel to a value of 7.6. According to amino-acid composition, the theoretical pI is 7.011. The effect of temperature on the endoglucanase activity, with carboxymethyl cellulose and amorphous cellulose as substrates, respectively, was studied at pH 5.5 and displayed an unusually broad optimum activity temperature range between 30 and 50 °C. Another unusual feature is that the enzyme retains 55,60% of its maximum activity at 0 °C. The enzyme readily degrades amorphous cellulose and carboxymethyl cellulose but displays no hydrolytic activity towards crystalline cellulose (Avicel) and shows no cross-specificity for xylan; there is no binding to Avicel. The enzyme can withstand 10 min at 100 °C without irreversible loss of enzymatic activity. Amino-acid sequence-based classification has revealed that the enzyme belongs to the glycoside hydrolase family 45, subfamily 2 (B. Henrissat, Centre de Recherches sur les Macromolecules Végétales, CNRS, Joseph Fourier Université, Grenoble, France, personal communication). [source] Isolation and identification of mixed linked , -glucan degrading bacteria in the intestine of broiler chickens and partial characterization of respective 1,3-1,4- , -glucanase activitiesJOURNAL OF BASIC MICROBIOLOGY, Issue 3 2006Lutz Beckmann Media with 1,3-1,4- , -glucans as selective markers were used for isolation of non-starch-polysaccharide (NSP) degrading bacteria from the intestinal tract of broiler chicken. Formerly unknown 1,3-1,4- , endoglucanase activities in various bacterial species were identified in this study. E. faecium , Streptococcus , Bacteroides and Clostridium strains seem to be responsible for degradation of mixed linked , -glucans in the small intestine and in the hind gut of chickens. Strict anaerobic bacteria (Bacteroides ovatus , B. uniformis , presumably B. capillosus and Clostridium perfringens ) as well as an unidentified bacterium with 98% 16S rDNA homology to an uncultered chicken cecum bacterium were isolated. Additionally, Streptococcus bovis with 1,3-1,4- , -endoglucanase activity was also detected. Different 1,3-1,4- , -endoglucanase activity profiles were observed in SDS/PAGE zymograms. (© 2006 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Pleomorphism of the marine bacterium Teredinobacter turniraeLETTERS IN APPLIED MICROBIOLOGY, Issue 1 2001G.M. Ferreira Aims:,A morphology transition for the marine bacterium, Teredinobacter turnirae is reported. Methods and Results:,When grown in the rod-shaped morphology, the cells require high concentrations of NaCl (0·3 mol l,1) and secrete extracellular protease and endoglucanase activity. When this bacterium is grown in a medium containing casein as a sole carbon and nitrogen source, a major change in morphology to a stable aggregated form is obtained. Conclusions:,In the aggregated morphology, much higher protease production rates (170 Units ml,1 d,1 for aggregates vs. 15 Units ml,1 d,1 for rods, for the same initial biomass) and negligible endoglucanase titres are obtained. In addition, the aggregated morphology does not require sodium chloride for growth. Significance and Impact of the Study:,The phenomenon reported here describes a novel relationship between the cell morphology and the biochemical characteristics of the bacterium. [source] | ||||||||||