Change of soybean isolate polypeptide composition during thermal inactivation of trypsin inhibitors
2000
Velickovic, D.P. | Vucelic-Radovic, B.V. | Barac, M.B. | Stanojevic, S.P. (Univerzitet u Beogradu, Beograd - Zemun (Yugoslavia). Poljoprivredni fakultet)
The change of polypeptide composition of soybean isolates, prepared from samples treated by autoclaving in the aim of trypsin inhibitors inactivation (0.5 bar; 5, 10 and 15 min.) was investigated. By densitometric analysis of SDS-PAGE-gels, the composition of soybean isolated protein was determined. According to our results, glycinin showed the highest content among proteins of soybean isolates. Depending on duration of soybeans heating, the percentage of glycinin in resulting isolate was 47.14-53.08%. High content of acidic (30.02-30.98%) and basic (15.12-18.24%) polypeptides of glycinin was registered. High content of alfa-subunit of beta-conglycinin was determined (11.49-8.99%). The presence of Bowman-Birk TI as well as lypoxigenase, was not registered in any of protein isolates.
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