Trypsin inhibitor activity in the field bean (Vicia faba L.)

1972 ◽  
Vol 23 (6) ◽  
pp. 679-684 ◽  
Author(s):  
B. J. Wilson ◽  
J. M. McNab ◽  
Hazel Bentley
Keyword(s):  
Vicia Faba ◽  
Trypsin Inhibitor ◽  
Trypsin Inhibitor Activity ◽  
Field Bean ◽  
Inhibitor Activity ◽  
Vicia Faba L

Trypsin inhibitors of fababeans (Vicia faba L. var. minor). 1. Preliminary studies.

1975 ◽  
Vol 53 (24) ◽  
pp. 3075-3077 ◽  
Author(s):  
R. S. Bhatty
Keyword(s):  
Vicia Faba ◽  
Trypsin Inhibitor ◽  
Crude Extract ◽  
Phosphate Buffer ◽  
Trypsin Inhibitors ◽  
Trypsin Inhibitor Activity ◽  
Boiling Water Bath ◽  
Inhibitor Activity ◽  
Ph Values ◽  
Vicia Faba L

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.

Trypsin inhibitor activity in vicia faba beans

1981 ◽  
Vol 7 (1) ◽  
pp. 63-71 ◽  
Author(s):  
A.Rafik El-Mahdy ◽  
E.K. Moustafa ◽  
M.S. Mohamed
Keyword(s):  
Vicia Faba ◽  
Trypsin Inhibitor ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity ◽  
Faba Beans

Characterization and trypsin inhibitor activity of proanthocyanidins from Vicia faba

1993 ◽  
Vol 34 (5) ◽  
pp. 1255-1260 ◽  
Author(s):  
Johannes P.F.G. Helsper ◽  
Johanna M. Hoogendijk ◽  
Arend van Norel ◽  
Herbert Kolodziej
Keyword(s):  
Vicia Faba ◽  
Trypsin Inhibitor ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity

TRYPSIN INHIBITOR ACTIVITY IN FABA BEANS (VICIA FABA VAR. MINOR), CHANGES DURING GERMINATION AND DISTRIBUTION

1977 ◽  
Vol 57 (3) ◽  
pp. 979-982 ◽  
Author(s):  
R. S. BHATTY
Keyword(s):  
Vicia Faba ◽  
Trypsin Inhibitor ◽  
Faba Bean ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity ◽  
Chick Pea ◽  
Faba Beans

Faba beans (Vicia faba var. minor L.) contained about the same level of trypsin inhibitor activity (TIA) as lentils and peas, ⅓ to [Formula: see text] that of vetch, chick pea and bean and about [Formula: see text] to [Formula: see text] that of flatpea and soybean. The TIA of faba bean increased two-fold during germination on the 3rd to 4th days after which it declined. The TIA was present mostly in the cotyledon fraction of faba bean.

Ileal digestibility of protein and amino acids of feed peas with different trypsin inhibitor activity in pigs

2000 ◽  
Vol 80 (4) ◽  
pp. 643-652 ◽  
Author(s):  
F. Grosjean ◽  
C. Jondreville ◽  
I. Williatte-Hazouard ◽  
F. Skiba ◽  
B. Carrouée ◽  
...  
Keyword(s):  
Amino Acids ◽  
Trypsin Inhibitor ◽  
Crude Protein ◽  
Trypsin Inhibitor Activity ◽  
Rectal Anastomosis ◽  
Inhibitor Activity ◽  
Ileal Digestibility ◽  
Physical Chemical ◽  
Protein Amino Acids ◽  
Weight Proportion

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

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