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Papain action

The use of papain in meat tenderization [70] is almost completely restricted to the United States. A number of techniques have been described (preslaughter as well as post slaughter administration) but are not always very successful. In all cases, papain action does not occur before the cooking of the meat and therefore the result is influenced by many factors other than the actual method of application. It has also been aiguedthat the use of papain in meat tenderizes, toothpaste, beer, and fruit juices is the main reason for the higher incidence of systemic allergic reactions after injection of chymopapain for treatment of sciatica in North America than in Europe. [Pg.118]

Feliu J, De Mas C, Lopez-Santin J (1995) Studies on papain action in the synthesis of Gly-Phe in two-liquid-phase media. Enzyme Microb Technol 17 882-887 Fihppova 1, Lysoeorskaya E (2003) Modified proteinases in peptide synthesis in organic media. Bioorg Khim 29(5) 544-550... [Pg.270]

The effect of pH upon the hydrolysis of several of these substrates is shown in Figure 15. The rates of hydrolysis were determined by the method of Grassmann and Heyde (66) at an arbitrarily selected substrate concentration of 0.05 M. In general, the optimum for papain action is near pH 7 but in some cases (BAA) there is a broad optimum from pH 5 to pH 7.5 (Fig. 17). [Pg.305]

R=Me or COOEt) failed.2-Amino-4-phosphonobutanoic acid, the phosphonic acid analogue of glutamic acid, has been obtained in resolved forms by the action of papain, followed by aniline, on 2-benzoylamino-4-(diethoxyphosphinyl)butanoic acid when anilide occurs preferentially for the L- compound. Enantiomers of 4-amino-4-phosphonobutanoic acid were obtained by resolution... [Pg.160]

Fig. 19 Structure of LA-PRX (above) and degradation of LA-PRX (below), (a) Threaded a-CDs prevent hydrolysis of PLLA in LA-PRX. (b) LA-PRX converts into LA-pPRX by peptide linkage cleavage at bulky end-capping groups through action of papain, (c) Ester bond hydrolysis in the PLLA chain begins by an exposure of PLLA to water by release of a-CDs from LA-pPRX. Reprinted from [292] with permission... Fig. 19 Structure of LA-PRX (above) and degradation of LA-PRX (below), (a) Threaded a-CDs prevent hydrolysis of PLLA in LA-PRX. (b) LA-PRX converts into LA-pPRX by peptide linkage cleavage at bulky end-capping groups through action of papain, (c) Ester bond hydrolysis in the PLLA chain begins by an exposure of PLLA to water by release of a-CDs from LA-pPRX. Reprinted from [292] with permission...
Fractionation of Wheat Gluten Complete acid hydrolysis of the gluten results in loss of its deleterious properties. Deamidation by acid or by treatment with papain (K6) also markedly reduces its toxic action on patients with gluten-induced enteropathy. However, peptic/tryptic digestion does not significantly reduce toxicity (F27). This might be expected from the fact that... [Pg.106]

Borio P (1953) The anthelmintic action of papain and of piperazine diphenylacetate (DPP). Minerva Farm 2(4) 141-142... [Pg.124]

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]

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]

K. I. Angeuoes and A. L, rink, Mechanism of action of papain with a specific anilide substrate. Biochemistry J 235J (1979),... [Pg.126]


See other pages where Papain action is mentioned: [Pg.123]    [Pg.303]    [Pg.123]    [Pg.123]    [Pg.303]    [Pg.123]    [Pg.437]    [Pg.174]    [Pg.807]    [Pg.207]    [Pg.208]    [Pg.373]    [Pg.71]    [Pg.324]    [Pg.24]    [Pg.241]    [Pg.293]    [Pg.201]    [Pg.324]    [Pg.1377]    [Pg.90]    [Pg.498]    [Pg.107]    [Pg.119]    [Pg.55]    [Pg.184]   
See also in sourсe #XX -- [ Pg.304 , Pg.305 ]




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