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Pepsin molecular weight

Pepsin consists of a single polypeptide chain of molecular weight 34 644 and 327 amino acid residues. Ser-68 is phosphorylated, but this phosphate may be removed without significantly altering the catalytic properties of the enzyme. As in other acid proteases, the active site is an extended area that can accommodate... [Pg.1]

The conditions necessary Tor the plastein reaction have been reviewed by Fujimaki et al. ( ), and compared to those necessary for proteolysis by Arai et al. ( ). The substrate for the synthetic reaction must consist of low molecular weight peptides, preferably in the tetramer to hexamer range. These are usually produced from proteins by protease action. A number of proteolytic enzymes and protein substrates have been investigated for producing plastein reaction substrates. The most often used proteases are pepsin JJ), and papain (12,13), but others... [Pg.277]

Pepsin Hydrolysis of polypeptides, including those with bonds adjacent to aromatic or dicarboxylic L-amino acid residues, yielding peptides of lower molecular weight. [Pg.151]

Many workers have studied the influence of enzymatic hydrolysis on the functional properties of various food proteins, and much of this work has recently been reviewed by Richardson (2). However, there seem to be very few reports which quantitatively relate functionality to parameters which characterize the protein hydrolysates per se (e.g. molecular weight). Ricks et al. (3 ) examined the solubility and taste of a number of pure proteins (denatured pepsin, lactoblobulin, a-Sj -, K-, and 8-casein) hydrolysed with... [Pg.125]

Molecular Weight. Detailed information on the molecular weights of pepsin from several species, chymosin, and fungal enzymes is given by Fruton (46) and Matsubara and Feder (29), They are in the range of 30,000-40,000 for the mammalian gastric proteins and microbial enzymes. A protease from Saccharomyces cerevisiae with a molecular weight of... [Pg.152]


See other pages where Pepsin molecular weight is mentioned: [Pg.138]    [Pg.262]    [Pg.427]    [Pg.807]    [Pg.184]    [Pg.451]    [Pg.455]    [Pg.506]    [Pg.316]    [Pg.372]    [Pg.806]    [Pg.49]    [Pg.99]    [Pg.614]    [Pg.1629]    [Pg.349]    [Pg.499]    [Pg.240]    [Pg.2]    [Pg.357]    [Pg.11]    [Pg.129]    [Pg.1]    [Pg.608]    [Pg.403]    [Pg.545]    [Pg.508]    [Pg.509]    [Pg.509]    [Pg.511]    [Pg.302]    [Pg.302]    [Pg.302]    [Pg.591]    [Pg.35]    [Pg.281]    [Pg.169]    [Pg.203]    [Pg.193]    [Pg.512]    [Pg.238]    [Pg.238]    [Pg.307]    [Pg.377]   
See also in sourсe #XX -- [ Pg.22 ]




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Pepsin

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