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Fungal protease

Baking Bread dough modification protease fungal 4,7,10... [Pg.98]

Chillproofing protease fungal, (Serial, papain, pepsin 10... [Pg.98]

From Sigma 3-aminoethylcarbazole (AEC) acrylamide/bis-acrylamide (30%) 37.5 1 amino acids alumina bentonite benzamidine bovine fiver tRNA bovine serum albumin (BSA) creatine phosphate (CP) diethyl pyrocarbonate (DEPC) dithiothreitol (DTT) Escherichia coli MRE600 tRNA pyrophosphatase (Ppase) Ca++ salt of folinic acid, (5-formyl THF) IIHPHS K salt of phospho-enol pyruvic acid, (PEP) creatine phospho kinase (CPK) protease inhibitor cocktail for fungal and yeast extracts phenylmethylsulfonyl fluoride (PMSF) spermidine trihydrochloride Tween 20. [Pg.262]

FIGURE 2 Examples of the variety of structures obtained in natural product screens. I, zaragozic acid A, is an inhibitor of mammalian and fungal sterol synthesis, obtained from fungi (48) II, L-696,474, is an inhibitor of the HIV protease, obtained from fungi (51) III, dehydrosoyasaponin I, is an agonist of the calcium-activated potassium channel, obtained from a medicinal plant (58) IV, tetrandrine, is an inhibitor of L-type calcium channels, obtained from a plant (78). [Pg.199]

Whereas standard proteases use serine, cysteine, aspartate, or metals to cleave peptide bonds, the proteasome employs an unusual catalytic mechanism. N-terminal threonine residues are generated by self-removal of short peptide extensions from the active yS-subunits and act as nucleophiles during peptide-bond hydrolysis [23]. Given its unusual catalytic mechanism, it is not surprising that there are highly specific inhibitors of the proteasome. The fungal metabolite lactacystin and the bacterial product epoxomicin covalently modify the active-site threonines and in-... [Pg.222]

Fungal and Yeast Protease CocktaiL These should contain the following inhibitors AEBSF, pepstatin A, E-64, and 1,10-phenanthroline. [Pg.578]

Apart from proteases, cutinases and lipases were demonstrated to hydrolyse PA. Hydrolysis of PA with a lipase (not further specified) was confirmed by using FTIR analysis and dye-binding assays [32]. Several reports have assessed the potential of cutinases for PA functionalisation, and a fungal cutinase from F. solani was successfully genetically engineered towards higher activity on a PA oligomer and PA [23-25]. [Pg.119]

Kirchgessner and Steinhart (52) studied the in vitro digestion of soy protein isolate with pepsin. They showed that a relatively higher percentage of the essential amino acids threonine, valine, isoleucine, leucine and phenylalanine were found in the undigested residue and therefore would be present in lower proportions in the hydrolysate. Myers et al. ( ) hydrolyzed a soy protein isolate with a fungal acid protease. They also found that the essential amino acid content of the hydrolyzate was lower than the isolate, but, as prepared by their continuous process, the hydrolyzate PER was not significantly reduced as compared to the isolate PER. [Pg.254]

Treatment of albumen with trypsin, bromelain and fungal protease produced significantly greater volumes of foam compared to stored control albumen (49). However, all enzyme treatments had inferior foam stability when compared to controls. Both the rate and amount of foam collapse was greater in enzyme-treated samples. The fresh control produced the most stable foam. [Pg.290]

Water Uptake and Retention. The water binding capacity of soy protein isolate can be increased by treatment with neutral fungal protease (20). Since the number of free amino and carboxyl groups increases as a result of digestion and because moisture uptake by proteins is proportional to the number of ionic groups present ( ), it is not surprising that moisture uptake is increased by enzyme treatment. [Pg.291]

Verma and McCalla ( ) studied the action of pepsin, papain and a commercial fungal protease on wheat gluten. All enzymes acted effectively on dispersed gluten however, the action of different enzymes produced different types of digestion products. Depending upon desired handling characteristics of bread doughs prepared from treated wheat flour, various types of protease treatments can be selected. [Pg.293]


See other pages where Fungal protease is mentioned: [Pg.36]    [Pg.12]    [Pg.17]    [Pg.520]    [Pg.36]    [Pg.12]    [Pg.17]    [Pg.520]    [Pg.285]    [Pg.36]    [Pg.47]    [Pg.292]    [Pg.253]    [Pg.270]    [Pg.63]    [Pg.172]    [Pg.111]    [Pg.506]    [Pg.198]    [Pg.126]    [Pg.175]    [Pg.155]    [Pg.128]    [Pg.72]    [Pg.72]    [Pg.63]    [Pg.28]    [Pg.608]    [Pg.615]    [Pg.118]    [Pg.224]    [Pg.225]    [Pg.118]    [Pg.70]    [Pg.167]    [Pg.103]    [Pg.106]    [Pg.284]    [Pg.285]    [Pg.288]    [Pg.289]    [Pg.290]   
See also in sourсe #XX -- [ Pg.54 , Pg.55 ]




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