Proteolise com a-quimotripsina do isolado proteico de soja maleilado

AUTOR(ES)
DATA DE PUBLICAÇÃO

2000

RESUMO

Chemical modification of soybean protein isolates (SPI) with maleic anhydride has not been studied to any great extent. The objective of the present work was to investigate the effect of maleylation of SPI on the total trypsin inhibitory activity, available lysine content, polyacrylamide-gel electrophoretic (SDS-PAGE) mobility, surface hydrophobicity of the SPI components and the effect on proteolysis of the isolate with a-chymotrypsin. The SPI suspension was reacted with maleic anhydride in the concentrations of (mole/L) 0.017 (SPIM1), 0.0505 (SPIM2), 0.0809 (SPIM3) and 0.1535 (SPIM4). For comparison, a sample of the isolate was thermally denatured at 80°C for 10 minutes. The SPI treatments showed corresponding lysine modification (maleylation) extents of (%) 3.2, 50.7, 86.7 and 92.4. Use of benzqyl-DL-arginine-p-nitroanylide (BAPNA) indicated that the levels of active inhibitor varied inversely with respect to the degree of maleylation and that, except for the least modified product, all of the chemical treatments were more effective at removing the antitryptic activity than thermal treatment ...Note: The complete abstract is available with the full electronic digital thesis or dissertations

ASSUNTO(S)

anidrido maleico solubilidade acilação peptidios hidrolise

ACESSO AO ARTIGO

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