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

Selection of food waste with low moisture and high protein content from Mexican restaurants as a supplement to swine feed

2020 ◽  
Vol 256 ◽  
pp. 120137 ◽  
Author(s):  
Liliana Fausto-Castro ◽  
Pasiano Rivas-García ◽  
Jesús Alfredo Gómez-Nafte ◽  
Ramiro Rico-Martínez ◽  
Vicente Rico-Ramírez ◽  
...  
Keyword(s):  
Protein Content ◽  
Food Waste ◽  
High Protein ◽  
High Protein Content ◽  
Swine Feed ◽  
Selection Of

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 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.

scholarly journals Proteins and Bioactive Peptides in High Protein Content Foods

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1186
Author(s):  
Fidel Toldrá ◽  
Leticia Mora
Keyword(s):  
Enzymatic Hydrolysis ◽  
Protein Content ◽  
Human Body ◽  
Bioactive Peptides ◽  
High Protein ◽  
Microbial Fermentation ◽  
Gastrointestinal Digestion ◽  
High Protein Content ◽  
By Products

Foods and their industry by-products constitute very good sources of bioactive peptides, which can be naturally generated during processing but are also extensively produced through enzymatic hydrolysis, microbial fermentation, and even during gastrointestinal digestion in the human body [...]

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

Sign in / Sign up

Export Citation Format

Share Document