scholarly journals The effect of autoclaving on soluble protein composition and trypsin inhibitor activity of cracked soybeans

2004 ◽  
pp. 49-57 ◽  
Author(s):  
Sladjana Stanojevic ◽  
Biljana Vucelic-Radovic ◽  
Miroljub Barac ◽  
Mirjana Pesic
Keyword(s):  
Protein Content ◽  
Soluble Protein ◽  
Protein Solubility ◽  
Residual Activity ◽  
Protein Composition ◽  
Extraction Methods ◽  
Nitrogen Solubility Index ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity ◽  
Kunitz Inhibitor

The effects of autoclaving conditions (heating for 5, 10 and 15 minutes at 0.5 bars over pressure) and oil-extracting temperatures (40?C, 60?C) on protein content, composition, and inhibitor activity of cracked soybeans were investigated. The results obtained indicated that oil-extracting method and heat treatment had significant influence on soluble protein content and composition. Raw soybean samples defatted at lower temperature had better solubility (535.42?2.10 mg/g) than those obtained by the Soxhlet procedure (345.53?2.80). The same results were obtained for nitrogen solubility index. Autoclaving combined with two oil-extraction methods decreased protein solubility to 180.32?1.50 -245.41?1.41 mg/g, while the dominant component of heat treated flours was 11S fraction. High content of glycinin fraction (44.59-41.10%) implies the possible use of treated samples in food industry. Residual activity of treated samples was 43.40-84.26%. Kunitz inhibitor (KTI) was responsible for residual inhibitor activity.

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
Keyword(s):  
Trypsin Inhibitor ◽  
Strong Dependence ◽  
Total Content ◽  
Human Consumption ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity ◽  
Soybean Genotype ◽  
Kunitz Inhibitor ◽  
Soybean Genotypes ◽  
The Impact

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.

scholarly journals Efecto de la cocción sobre algunas características nutricionales del frijol

2016 ◽  
Vol 4 ◽  
pp. 42 ◽  
Author(s):  
Carmen Jacinto Hernández ◽  
Albino Campos Escuerdo
Keyword(s):  
Protein Content ◽  
Trypsin Inhibitor ◽  
Cooking Time ◽  
Crude Fiber ◽  
Chemical Components ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity ◽  
Tryptophan Content ◽  
Low Activity

Seven bean varieties of the seed types: Flor de Mayo, Negro, Bayo, and Canario, and the line BAT 104 were included in this study. The objective of this research was to analyze the technological and nutritive characteristics as well as the changes that result from cooking in the digestibility and the activity of the trypsin inhibitor of the materials. Highly significant differences among varieties in weight, volume, coat percentage, cooking time, trypsin inhibitor activity and digestibility were found. The protein content in the materials ranged from 22.6 to 27.3 %. Also, differences were detected among materials in the chemical components such as starch, crude fiber, ash, lysine and tryptophan content. A low activity of the trypsin inhibitor in cooked beans was more correlated with longer cooking time and smaller grains rather than with the inhibitor content in raw beans. Digestibility of the materials was increased 11% on the average as a consequence of cooking.

scholarly journals Selection of Sweetpotato Lines with High Protein Content and/or Low Trypsin Inhibitor Activity

2006 ◽  
Vol 56 (1) ◽  
pp. 17-23 ◽  
Author(s):  
Jun Toyama ◽  
Makoto Yoshimoto ◽  
Osamu Yamakawa
Keyword(s):  
Protein Content ◽  
Trypsin Inhibitor ◽  
High Protein ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity ◽  
High Protein Content ◽  
Selection Of

Effect of variety on protein content, amino acid composition and trypsin inhibitor activity of cowpeas

1988 ◽  
Vol 29 (1) ◽  
pp. 65-78 ◽  
Author(s):  
Neena Kochhar ◽  
Ann F. Walker ◽  
Derek J. Pike
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Protein Content ◽  
Acid Composition ◽  
Trypsin Inhibitor ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity

scholarly journals MOLECULAR PROFILE, PURITY AND PRESENCE OF TRYPSIN INHIBITORS IN COWPEA PROTEIN ISOLATES

2018 ◽  
Vol 31 (1) ◽  
pp. 202-208
Author(s):  
KAROLINE DE MACÊDO GONÇALVES FROTA ◽  
LAYS ARNAUD ROSAL LOPES ◽  
IZABEL CRISTINA VERAS SILVA ◽  
JOSÉ ALFREDO GOMES ARÊAS
Keyword(s):  
Protein Content ◽  
Trypsin Inhibitor ◽  
Extraction Yield ◽  
Raw Material ◽  
Molecular Profile ◽  
Trypsin Inhibitor Activity ◽  
Inhibitor Activity ◽  
Isoelectric Precipitation ◽  
Protein Isolates ◽  
Kjeldahl Method

ABSTRACT The most-used preparation process of protein isolates (PI) involves the isoelectric precipitation of the protein. Heating shortens the preparation time but this procedure may affect the purity, yield, molecular profile of the protein, and the activity of the trypsin inhibitor. This study aimed to investigate the effect of heating in the production of cowpea protein isolates. Crude whole beans (WB) were defatted with hexane, and the protein isolates obtained by isoelectric precipitation with (HPI), and without (NHPI) heating. The protein content of the WB and the PI was determined by the micro-Kjeldahl method, and the extraction yield estimated from the protein content at the end of extraction in relation to this content in the raw material. Possible losses of protein fractions were followed by SDS-PAGE, and the trypsin inhibitor activity determined by an enzymatic assay (BAPNA: benzoyl-DL-arginine-p-nitroanilide). Protein content in HPI was 83.3%, less than in the NHPI (92.2%). The HPI yield was lower (40.0%) as compared to the NHPI (42.3%). Electrophoresis indicated bands ranging from 13 to 262 kDa in WB; and the NHPI presented a protein fraction’s profile closer to that of the WB than to the HPI. The WB had the trypsin inhibitor activity, expressed as Trypsin Inhibitory Units (TIU), of 32.5±0.5 TIU /mg-protein; HPI showed 12.7±0.5 TIU /mg-protein (39% of that observed in WB) and the NHPI, 8.3±0.2 TIU /mg-protein (25.5%). Heating reduces the yield and purity of proteins in the isolates. However, the inhibitory activity of trypsin cowpea is most affected by the isolation procedure.

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