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Enzymes of celluloses

Strain improvement can be better if the overproduction of desired product can be from wide and unconventional substrate range. WeU-established amino acid overproducers are further engineered to utilize lignocellulose-derived sugars. One step further, enzymes of cellulose degradation are incorporated leading to one-step bioconversion from cellulose to amino acids. [Pg.454]

The enzyme catalyst used for the reaction is cellulase, an extracellular hydrolysis enzyme of cellulose. The enzyme promotes transglycosylation of the cellobiosyl moiety toward the 4 hydroxyl group of another cellobiosyl fluoride eliminating hydrogen fluoride. The polymerization was carried out in aqueous... [Pg.17]

Animals lack fhe enzymes necessary fo cafalyze fhe hydrolysis of cellulose and so can 1 digesf if Caffle and ofher rummanfs use cellulose as a food source mdirecfly... [Pg.1048]

Alcoholic Fermentation. Certain types of starchy biomass such as com and high sugar crops are readily converted to ethanol under anaerobic fermentation conditions ia the presence of specific yeasts Saccharomyces cerevisia and other organisms (Fig. 6). However, alcohoHc fermentation of other types of biomass, such as wood and municipal wastes that contain high concentrations of cellulose, can be performed ia high yield only after the ceUulosics are converted to sugar concentrates by acid- or enzyme-catalyzed hydrolysis ... [Pg.18]

With respect to the action of the enzyme itself, a loss of weight on account of cellulose hydrolysis, as well as loss in strength properties, occurs. Therefore, control of concentrations, temperature, and other processing conditions is important to achieve a product having the proper balance of properties. [Pg.447]

Increasingly, biochemical transformations are used to modify renewable resources into useful materials (see Microbial transformations). Fermentation (qv) to ethanol is the oldest of such conversions. Another example is the ceU-free enzyme catalyzed isomerization of glucose to fmctose for use as sweeteners (qv). The enzymatic hydrolysis of cellulose is a biochemical competitor for the acid catalyzed reaction. [Pg.450]

More recently, interest has developed in the use of enzymes to catalyze the hydrolysis of cellulose to glucose (25—27). Domestic or forest product wastes can be used to produce the fermentation substrate. Whereas there has been much research on alcohol fermentation, whether from cereal grains, molasses, or wood hydrolysis, the commercial practice of this technology is primarily for the industrial alcohol and beverage alcohol industries. About 100 plants have been built for fuel ethanol from com, but only a few continue to operate (28). [Pg.450]

Historically, dietary fiber referred to iasoluble plant cell wall material, primarily polysaccharides, not digested by the endogenous enzymes of the human digestive tract. This definition has been extended to iaclude other nondigestible polysaccharides, from plants and other sources, that are iacorporated iato processed foods. Cellulose [9004-34-6] (qv) is fibrous however, lignin [9005-53-2] (qv) and many other polysaccharides ia food do not have fiberlike stmctures (see also Carbohydrates). [Pg.69]

Cellulase The enzyme that cuts the linear chain of cellulose, a glucose polymer at 1-4-p-linkages into cellodextrins and glucose. [Pg.901]

The glycosidic bond to an anomeric carbon can be either a or (3. Maltose, the disaccharide obtained by enzyme-catalyzed hydrolysis of starch, consists of two cv-D-glucopyranose units joined by a 1->4-o-glycoside bond. Cellobiose, the disaccharide obtained by partial hydrolysis of cellulose, consists of two /3-o-glucopyranose units joined by a 1—>4-/3-glycoside bond. [Pg.998]

The plant cell wall is a polymeric mesh consisting of cellulose, hemicellulose, pectin and protein. Cellulose and hemicellulose are integral components of the cell wall, but pectic substances are located mainly in the outer wall regions within the middle lamella (McNeil et ai, 1984). Pectic substances are more susceptible to enzymatic degradation, because they are more exposed than other cell wall components. Therefore, pectin-degrading enzymes may play a central role in the penetration of plant tissue by bacteria. [Pg.378]

Berg R. H., G. W. Erdos, M. Gritzali and R. D. Brown. (1988). Enzyme-gold affinity labeling of cellulose. Journal of Electron Microscopy Techniques 8 371-379. [Pg.736]

Enzymes have traditionally been closely associated with the desizing of cellulosic fabrics. In recent years, however, the sphere of possible, if not actual, uses has widened considerably. [Pg.81]

In one study [90], enzyme pretreatment increased colour yield without affecting fastness properties. However, pretreatment of cellulosic fibres with cellulase lowered the subsequent fixation of homobifunctional triazine reactive dyes but did not impair the fixation of other types of reactive dyes [91]. Another study suggested that the enhanced brightness of reactive dyeings was greater with triazine dyes than with vinylsulphone types when cotton was pretreated or aftertreated with cellulase [92]. [Pg.83]

Y. Kurokawa, T. Sano, H. Ohta, and Y. Nakagawa, Immobilization of enzyme onto cellulose-titanium oxide composite fiber. Biotech. Bioenerg. 42, 394—397 (1993). [Pg.551]

A new generation of cheap enzymes for hydrolysis of cellulose and lignocellu-lose to fermentable sugars (able to complete the biomass hydrolysis during fermentation). [Pg.189]

Further research is also needed in this area. Particularly, (a) to create a new generation of cheap enzymes for hydrolysis of cellulose and lignocellulose to fermentable sugars (able to complete the biomass hydrolysis during fermentation) (b) to develop improved biocatalysts that allow us to simplify the process and reduce energy input and (c) to improve separation and recovery. [Pg.191]


See other pages where Enzymes of celluloses is mentioned: [Pg.261]    [Pg.21]    [Pg.50]    [Pg.168]    [Pg.2619]    [Pg.261]    [Pg.21]    [Pg.50]    [Pg.168]    [Pg.2619]    [Pg.155]    [Pg.296]    [Pg.447]    [Pg.303]    [Pg.222]    [Pg.231]    [Pg.162]    [Pg.84]    [Pg.335]    [Pg.335]    [Pg.931]    [Pg.111]    [Pg.667]    [Pg.82]    [Pg.82]    [Pg.5]    [Pg.353]    [Pg.79]    [Pg.157]    [Pg.100]    [Pg.208]    [Pg.60]    [Pg.391]    [Pg.319]    [Pg.766]    [Pg.10]    [Pg.196]   
See also in sourсe #XX -- [ Pg.8 ]




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