scholarly journals The influence of soybean genotypes and HTC processing method on trypsin inhibitor activity of soymilk

2016 ◽  
Vol 61 (3) ◽  
pp. 271-279 ◽  
Author(s):  
Sladjana Stanojevic ◽  
Miroljub Barac ◽  
Mirjana Pesic ◽  
Biljana Vucelic-Radovic

Kunitz inhibitor (KTI) and Bowman-Birk trypsin inhibitor (BBI) are inhibitors of digestive enzymes in raw soybeans. Due to their antinutritive properties in the active state, their inactivation by heat treatment is commonly used. Soymilk is a turbid and stable colloidal solution, obtained by thermal treatment of soybean. In this study soymilk was made on a pilot-plant scale from six soybean cultivars using hydrothermal cooking (HTC) as the production method. This procedure is significantly different from the traditional one. The aim of this investigation was to evaluate the impact of the HTC processing for soymilk production and different soybean genotypes on trypsin inhibitor content and activity. Obtained soymilk contained BBI in trace amounts, in the BBI-polymeric forms. The BBI monomeric forms were not detected. The soymilk of the investigated soybean genotypes had very similar KTI levels (2.34-2.99%). Results have suggested that the soybean genotype does not have substantial effects on the levels of KTI, as well as on the value of residual trypsin inhibitor activity (rTIA). The total content of TI and rTIA showed a strong dependence (r=0.91; p<0.05). HTC-soymilk rTIA was <20% (7.15-19.89%). These results have indicated that HTC processed soymilk is applicable for human consumption.


2021 ◽  
Vol 13 (1) ◽  
pp. 10836
Author(s):  
Priyanka MITTAL ◽  
Vineet KUMAR ◽  
Anita RANI ◽  
S. M. GOKHALE

Bowman-Birk inhibitor (BBI) is a soybean seed serine protease inhibitor whose nutraceutical properties far exceed its anti-nutritional property arising from its trypsin and chymotrypsin inhibitor activity. High BBI soybean genotypes are sought for the commercial preparation of this nutraceutical biomolecule while low BBI content in Kunitz trypsin inhibitor (KTI)-free genetic background is desirable in soymeal manufacturing. In the present investigation, monoclonal antibody assay of 95 soybean genotypes revealed 11-fold genetic variation for BBI concentration. The study led to the identification of 3 very high (>20 mg/g defatted soy flour) and 5 very low BBI (< 4 mg/g defatted soy flour) soybean genotypes. Contribution of BBI to total trypsin inhibition activity ranged from 2.2 to 53.5% with average value of 11.6%. Genotypes with varying level of BBI raised consecutively for two years exhibited non-significant (p>0.05) effect of growing year on the trait. BBI content in BC3F2 derived KTI-free lines was at par with the recurrent parent. Low and high BBI content genotypes with diverse genetic background identified in the study may be exploited to develop mapping population to identify genomic regions underlying BBI in soybean.



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


1995 ◽  
Vol 43 (8) ◽  
pp. 2231-2234 ◽  
Author(s):  
Juana Frias ◽  
Concepcion Diaz-Pollan ◽  
Cliff L. Hedley ◽  
Concepcion Vidal-Valverde


2016 ◽  
Author(s):  
Vesna Župunski ◽  
Vesna Spasić Jokić ◽  
Mirjana Vasić ◽  
Aleksandra Savić ◽  
Zoran Mitrović ◽  
...  


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