Trypsin Inhibitor Assay: Expressing, Calculating, and Standardizing Inhibitor Activity in Absolute Amounts of Trypsin Inhibited or Trypsin Inhibitors

2021 ◽  
Vol 98 (4) ◽  
pp. 355-373 ◽  
Author(s):  
Keshun Liu

1975 ◽  
Vol 53 (24) ◽  
pp. 3075-3077 ◽  
Author(s):  
R. S. Bhatty

Trypsin-inhibitor activity (TIA) of three cultivars of fababeans was compared with that of soybean. A 50 mM phosphate buffer, pH 7.6, extract of soybean contained 35 times more specific TIA than similarly prepared extracts of fababeans. The fababean trypsin inhibitors (TI), like those of soybean, were highly thermostable. The crude extract possessed 13 to 20% of the original inhibitor activity after heating in a boiling water bath for 60 min. The total TIA was higher in extracts of phosphate (pH 7.6) and of ammonium formate (pH 3.2) than of acetate (pH 4.6). However, the specific TIA of the lower pH extracts was higher as a result of a reduced solubility of the fababean proteins at these pH values.



2000 ◽  
Vol 80 (4) ◽  
pp. 643-652 ◽  
Author(s):  
F. Grosjean ◽  
C. Jondreville ◽  
I. Williatte-Hazouard ◽  
F. Skiba ◽  
B. Carrouée ◽  
...  

Ileal digestibility of protein and amino acids was measured in pigs fed 13 round, tannin-free peas samples and related to the following physical, chemical and biological characteristics of these samples: thousand-seed weight, proportion of hulls, starch, fibre, crude protein, ether extract and ash contents, trypsin inhibitor activity and trypsin inhibitor activity per unit of crude protein (TIAP). Each pea sample was included in a diet containing starch, sucrose, minerals and vitamins and fed to four barrows (50 to 100 kg) fitted with an end-to-end ileo-rectal anastomosis. Standardised ileal protein and amino acid digestibilities, except for alanine of peas decreased linearly with increasing TIAP (P < 0.01) and was not affected by fiber content. For example standardized ileal digestibilities values (%) decreased by −0.1975, −0.1617, −0.2171, −0.2630, −0.2029 and −0.3536 per unit of TIAP (expressed in unit of trypsin inhibited per milligram crude protein), respectively, for crude protein and lysine, threonine, methionine, cystine and tryptophan. Key words: Peas, trypsin inhibitor activity, standardised ileal digestibilities, protein, amino acids, pig



2005 ◽  
Vol 7 (1) ◽  
pp. 17-23 ◽  
Author(s):  
Jun Toyama ◽  
Makoto Yoshimoto ◽  
Osamu Yamakawa


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