Cellulases processing

Paulo, A. C., and Almeida, L. (1996]. Kinetic parameters measured during cellulase processing of cotton. /. Text Inst. 1(4], 227-233. 

Enzymatic liquefaction is a relatively new process for the production of juices from fruits and vegetables [1]. Essentially the process is as follows the material is crushed to obtun a pulp which is treated with a combination of pectinases and cellulases. After a certain incubation time, the material becomes a liquid and the Juice can be recovered by decantation. 

Biofinishing, or biopolishing as it is more popularly known, is similar to denim washing in its use of cellulase enzymes, although the effects intended are quite different. The process is designed to eliminate, by dissolution, the cellulosic fibrils projecting from the surface of the fabric. This treatment results in [76] ... 

The precise effects obtained are dependent on the fabric quality, the type of cellulase enzyme and the application conditions, but no mechanical forces are involved in removal of the fibrils. The process has attracted considerable attention and is now one of the main methods of defibrillating lyocell fabrics [94,101-114]. Simultaneous treatment with cellulase and protease enzymes has been applied to the biofinishing of wool/cotton blends [115]. 

As surfactants are often used in textile processing, it is important to note that anionic or cationic surfactants can inhibit the action of enzymes, as has been reported in the case of cellulases used for the treatment of cotton [140]. Dyes can also inhibit enzyme activity for example, Cl Direct Red 28 has been shown to have a much greater inhibitory effect than Cl Acid Orange 7 [141]. 

Enzink [Enzyme deinking] A paper deinking process using cellulase enzymes. Invented by K.-E. L. Eriksson and J. L. Yang at the University of Georgia and commercialized in 1994. 

FIG. 1 Effect of different enzymes or combination of enzymes (cellulases, xylanases, cellobiases, 3-glucanases, and proteases) on starch yield in the conventional corn wet milling process. 

The anaerobic biological conversion of the major polymeric components of MSW identified require appropriate microorganisms and hydrolytic enzyme systems. Extracellular hydrolytic enzymes, such as cellulases and lipases, have been shown to be effective in the post hydrolysis of anaerobic digester efQuent solids 34) or pretreatment of complex organic polymers before the digestion process 48),... 

Both digester systems exhibit extremely low levels of detectable cellulase activities (exoglucanase, endoglucanase, and -glucosidase) when compared to industrial saccharifying processes (See Table III) in which the hydrolysis of cellulose in the feedstock is optimized with respect to enzyme loading. Therefore, the data indicate the level of improvement that may be made to attain maximum rates for cellulose hydrolysis in the anaerobic reactor system. 

Current data indicate that the analysis of cellulase enzyme activities may be the best method for determining the projected cellulose conversion of the overall system, and therefore the hydrolytic power of the system under evaluation. With development, the analysis of enzyme activities may also serve as a "real time" method of monitoring the stability of the system, with radical changes in enzyme activities indicative of potential process upset. 

A literature survey indicated that very little work has been done to produce an optimal cellulase system as described above. Here, we used solid-state fermentation (SSF) to achieve this objective. SSF processes, such as the "koji" process, have been used extensively for amylase production on wheat bran in Japan its application was extended to cellulase production on wheat bran and Ugnocellulosic materials by Toyama (13), Since then, wheat bran has become an important substrate for producing various products by SSF (14-20), In this study, we tested various lignocellulosic substrates for the production of cellulase and )3-glucosidase from T, reesei QMY-1 by SSF. 

Cost sensitivity studies have shown that the successful commercialization of cellulase-based processes, such as the conversion of cellulose to fermentable sugars, is highly dependent on the cost of enzyme production (i). Because fungal -D-glucosidase (EC 3.2.1.21) is the most labile enzyme in this system under process conditions (2), and k to efficient saccharification of cellulose, this enzyme was targeted for application of stabilization technology, both through chemical modification and immobilization to solid supports. 

It is now apparent that many bacterial cellulases are composed of two or more structural and functional units or domains and it has been suggested that such enzymes arose by a process of domain shuffling (1). The domains may be catalytic or non-catalytic and their occurrence is often indicated in the primary protein structure by an intervening... 

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