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A Comparison of the ISO and AACC Methods for Determining the Activity of Trypsin Inhibitors in Soybean Meal
Author(s) -
Sueiro S.,
Hermida M.,
González M.,
Lois A.,
RodríguezOtero J. L.
Publication year - 2015
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-015-2702-8
Subject(s) - trypsin , chemistry , soybean meal , food science , kunitz sti protease inhibitor , trypsin inhibitor , meal , chromatography , significant difference , enzyme , biochemistry , organic chemistry , medicine , raw material
The international standard method for the determination of trypsin inhibitor activity (TIA) in soya products, ISO 14902, was compared with the American Association of Cereal Chemists’ standard AACC 22‐40.01 as modified by Hamerstrand in 1981 (AACC‐based method), using soybean meals as matrices. TIA, expressed as milligram of inhibited trypsin per gram of sample, was determined by both methods in each of 30 samples of soybean meal. TIA values according to ISO 14902 were significantly lower ( P < 0.001) than those afforded by the AACC‐based method. This difference, which means that AACC‐based method and ISO 14902 TIA values are not directly comparable, is attributable to between methods differences, in decreasing order of influence: particle size ( P < 0.01), trypsin inhibitor extraction method ( P < 0.05), and trypsin substrate ( P < 0.01). N ‐benzoyl‐ l ‐arginine‐4‐nitroanilide hydrochloride, the ISO 14902 trypsin substrate, affords TIA values 6.4 % higher than the racemic mixture used by the AACC method, but it seems unlikely that in most contexts this advantage would outweigh the disadvantage of its greater cost.