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Cellulase Aspergillus niger

Enzyme solution Aspergillus niger cellulase obtained from the Industrie Biologique Frangaise. The concentration in the reaction mixture equals 3.25 X 10 3 mg/mL. [Pg.124]

Pancreatic preparations have been widely used as digestive aids, because they contain proteases, amylase and lipase. They have been prescribed for patients who have pancreatic disorders or after removal of the pancreas. The various activities present in the pancreatic preparations can be duplicated by in vitro methods from blends of microbial enzymes derived from Bacillus subtilis, Aspergillus flavus-oryzae and Aspergillus niger. Cellulase derived from Aspergillus niger is often added to the microbial preparation. The pancreatic preparations still hold the major share of the market, but this could be a useful application for the right combination of microbial enzymes. [Pg.103]

Immobilization of Aspergillus niger cellulase on a polyacrylonitrile derivative raised the pH optimum of the enzyme by 0.4 units and lowered the temperature optimum by The pH-activity profile of the enzyme also narrowed on... [Pg.512]

Enzyme (3-glucosidase, almond-isolate or cellulase, Aspergillus niger extract... [Pg.1297]

Sprucewood holocellulose was treated with an endo-p-1,4-mannanase isolated from Aspergillus niger and an endo-/3-1,4-xylanase, two avicelases, and a cellobiohydrolase C isolated from Trichoderma viride. The mannanase hydrolyzed about a quarter of the mannan in 2-3 days without xylan or cellulose degradation. The xylanase hydrolyzed about half the xylan with 10% mannan solubilization. The three cellulases hydrolyzed up to 45% of the cellulose and 20% of the xylan, accompanied by 40-70% solubilization of the mannan. Combined xylanase-mannanase treatment hydrolyzed about half the xylan and mannan. Addition of mannanase to to cellulose-treated samples increased the degradation of the cellulose and mannan. Micromorphological studies of the variously treated specimens revealed a loss of substances in P/Slf T, and adjacent zones of S2 of the tracheid wall. [Pg.301]

From rate and product studies with xylooligosaccharides it was concluded that a xylanase from Ceratocystis paradoxa requires a chain of at least five xylose residues for rapid binding and subsequent hydrolysis (18). The catalytic site is assumed to be situated asymmetrically within a row of the five binding subsites. Similar studies on a cellulase from Aspergillus niger also suggest the presence of five binding subsites (14). [Pg.359]

From kinetic (57) and chemical modification (58) studies, Hurst et al. concluded that the catalytic residues in a cellulase from Aspergillus niger are a carboxylate anion (pKa 4.0-4.5) and a protonated carboxyl group (pKa 5.0-5.5) with tryptophan and dicarboxylic amino acid residues involved in substrate binding. [Pg.366]

Cellulase carbohydrase (1) Aspergillus niger var. (2) Trichoderma longibrachiatum (formerly reesei) Endo-l,4-(l,3 l,4)-(3-D-glucan 4-glucanohydrolase 3.2.1.4... [Pg.896]

Fig. 7. Distribution of protein and enzyme activity after filtration of cellulase from Aspergillus niger on Sephadex G-100. Column dimensions, 1.5 X 38 cm buffer,... Fig. 7. Distribution of protein and enzyme activity after filtration of cellulase from Aspergillus niger on Sephadex G-100. Column dimensions, 1.5 X 38 cm buffer,...
CellCept mycophenolic acid, cellulase [usan] is a concentrate of cellulose-splitting enzymes, isolated from Aspergillus niger. It is used as an adjunct DIGESTIVE AGENT. [Pg.70]

Most cellulase used in the juice industry is Trichoderma cellulase, because of the typically low pH present in the mash. Cellulase from Aspergillus niger is also used. [Pg.48]

Beta-glucosidase is available within the complex mixture of crude cellulase enzymes. In addition, some microbes, including Aspergillus niger, produce beta-glucosidase with httle additional cellulase activity. [Pg.55]

T Tses for cellulase have been found (34, 35, 36), and more ambitious proposals wait only on a supply of enzyme of sufficient activity, stability, and economy. Companies like Wallerstein, Miles, and Rohm and Haas in the United States and Meiji Seika and Kinki Yakult in Japan are marketing cellulases derived from Aspergillus niger, Trichoderma viride, and other organisms. While these preparations are good, they are limited both in rate and in extent of action on solid cellulose. [Pg.399]

Over 100 liters of active cellulase filtrate was harvested. After 60 days the culture became contaminated (with Aspergillus niger) and the yield declined. Other fermenters have maintained a good yield of cellulase for over 90 days without contamination. [Pg.417]


See other pages where Cellulase Aspergillus niger is mentioned: [Pg.99]    [Pg.340]    [Pg.369]    [Pg.387]    [Pg.99]    [Pg.340]    [Pg.369]    [Pg.387]    [Pg.353]    [Pg.923]    [Pg.925]    [Pg.964]    [Pg.1222]    [Pg.399]    [Pg.290]    [Pg.276]    [Pg.1296]    [Pg.303]    [Pg.111]    [Pg.393]    [Pg.148]    [Pg.2357]    [Pg.98]    [Pg.111]    [Pg.283]    [Pg.333]    [Pg.49]    [Pg.262]    [Pg.250]    [Pg.371]    [Pg.1498]    [Pg.1498]    [Pg.1498]    [Pg.58]    [Pg.367]    [Pg.367]    [Pg.368]    [Pg.184]    [Pg.185]   
See also in sourсe #XX -- [ Pg.95 , Pg.107 , Pg.120 ]

See also in sourсe #XX -- [ Pg.176 ]




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