Streptomyces cellulase

Cellulomonas fimi Endoglucanase A (i7) Microbispora bispora Endoglucanase I (5) Streptomyces sp. Cellulase A (72) Trichoderma reesei Cellobiohydrolase II (75)... 

Davies JL, Nakatsubo F, Murakami K, Umezawa T (1987) Organic acid pulping of wood IV Reactions of arylglycerol fi guaiacyl ethers Mokuzai Gakkaishi 33 478-486 Deobald LA, Crawford DL (1987) Activities of cellulase and other extracellular enzymes during lignin solubilization by Streptomyces vindosporus Appl Microbiol Biotechnol 26 158-163... 

The data further suggest that Chrysosporium pruinosum, and Pent-ctllium pusillum are good sources of exo-/ -l — 4 enzyme, if one does not object to the cellobiase present. Polyporus cinnabarinus produces less exo-enzyme, but as in Trichoderma viride, it is nearly free of cellobiase. Streptomyces sp. B814 is the only organism which appears to lack exo-glucanase in its cellulase complex. 

Product Inhibition. In most microbiological and biochemical systems accumulation of end products exercises an inhibitory effect on the rate of the forward reaction. Stimulation by end product is thermodynamically improbable. One of the major products of hydrolysis of cellulose is cellobiose. There is a stimulation by cellobiose of Cx activity of Streptomyces spp. filtrates only when the substrate is solubilized by the introduction of various substituents—e.g., CMC, hydroxycellulose, cellulose acetate, etc. Stimulation is absent when unsubstituted cellulose is used (14). On the other hand, product inhibition is common. Cellobiose inhibits the hydrolysis of cellulose by filtrates of most of the 36 organisms tested. This action of cellobiose is believed to be that of an end product inhibiting an enzymatic hydrolysis in much the same manner that maltose inhibits hydrolysis of starch by a-amylase. The inhibitory effect of products varies with the organism from which the cellulase is derived. Thus, lactose is a very good inhibitor of the enzyme from... 

Degradation of oat and barley glucans with Streptomyces cellulase, which produces mainly cellobiose and cellotriose from cellulose, resulted in production of a trisaccharide fraction and a tetrasaccharide fraction as the major products. These were isolated by preparative paper-chromatography, and the trisaccharide was found to preponderate ... 

Cellulase-producing bacteria include CelMomonas, Clostridium, Pseudomonas, Streptomyces, Thermonospora, and Ruminococcus, but bacterial cellulases digest cotton fibers to lower levels compared to amorphous celluloses (Ray et al., 2006). Cellulases have two functionally distinct domains in their structure, namely catalytic domain and cellulose substrate binding domain, linked by an interdomain, glycosylated linker peptide at either the N or the C terminal of the protein cellulose binding domains exhibit different affinities, specificities, some binding to crystalline cellulose, while others restrict themselves to the disordered regions. Catalytic domain has an active site in the shape of a tunnel or cleft where hydrolytic reactions take place (Cavedon et al., 1990 Lee et al., 1996). 

Jang HD, Chang KS. (2005). Thermostable cellulases from Streptomyces sp. scale-up production in a 50-L fermenter. Biotechnol Lett, 27, 239-242. 

Extracellular polysaccharides from Rhizobium trifolii, R. phaseoli, R. leguminosarum, and R. meliloti have been reduced and deacetylated. The resistance of the native polysaccharide to attack by Streptomyces cellulase (E.C. 3.2,1.4) or Rhizopus arrhizus laminarinase (E.C. 3.2.1.6) is lost on chemical modification. Results were discussed in relation to the available data on the structure of the polysaccharides and the specificity of the enzymes. 

Ishague, M., Kluepfeld, D., 1980, Cellulase complex of a mesophilic Streptomyces strain. Can. J. Microbiol. 26 183. 

A derivatized form of pneumococcal type III polysaccharide has been used to distinguish between three jS-D-glucan hydrolases (including cellulase) from a Streptomyces species. Oligosaccharides also released from carboxymethyl-cellulose, lichenin, and oat glucan by the enzymes were identified, allowing the substrate specificities of the enzymes to be deduced. 

An oligosaccharide from Streptomyces diastaticus has been shown to inhibit a-amylase. The oligosaccharide, which consists mainly of o-glucose, inhibited microbial and mammalian a-amylases and glucoamylase, but not jS-amylase, a-D-glucosidase, dextranase, cellulase, or -o-glucosidase. 

Kluepfel D, Shareck E, Mondou E, Morosoli R (1986) Characterization of cellulase and xylanase activities of Streptomyces lividans. Appl Microbiol Biotechnol 24 230-234... 

Hsu,C. L, Chang, K. S.,Lai,M. Z, Chang, T. C., Chang, Y.H., Jang, H.D.Pietreatment and hydrolysis of cellulosic agricultural wastes with a cellulase-producing Streptomyces for bioethanol production. Biomass and Bioenergy 2011, 35,1878-1884. 

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