Fungal degradation types

Bacterial, plant, and fungal enzymes for degradation/modification of polysaccharides left-hand-twisted /8-solenoid with L-type cross section... 

More information is needed on factors such as optimal cultures for specific applications, aeration, mixing requirements, timing of microbial and nutrient augmentation, soil type, and bioavailability of hazardous compounds. These parameters will help develop fungal composting as a reliable method for degrading PAHs. 

Where the juice is destined for concentration it is essential for the pectin to be destroyed, or degraded, as already mentioned. Pectinase or poly(l,4-a-D-galacturonide) glycanohydrolase, in its commercially available form, is produced from fungal sources (i.e. Aspergillus sp., Rhizopus sp.). and possesses a wide variety of component activities. It operates comfortably between pH 2.5 and 6.0 and subject to supplier type can function well at specified temperatures between 30 and 60°C. Activities include... 

Fungal cellulase enzyme systems capable of efficiently catalyzing the hydrolytic degradation of crystalline cellulose are typically composed of endo-acting cellulases (EGs), exo-acting cellulases (CBHs), and at least one cellobiase (1-6). The CBHs are typically the predominant enzymes, on a mole fraction basis, in such systems (7). Consequently, the CBHs have been the focus of many studies (8). The three-dimensional structure of prototypical CBHs is known (9-12) and their specificities are, in general, well characterized (13,14). However, mechanism-based kinetic analyses of CBH-catalyzed cellulose saccharification are rather limited (15,16). Studies of this latter type are particularly difficult owing to the inherent complexity of native cellulose substrates. 

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