EFFECTS OF VARIOUS HEAT AND pH TREATMENTS ON DIGESTIBILITY OF PROTEIN IN PEA PROTEIN CONCENTRATE (PISUM SATIVUM)

Pea protein concentrate (PPC) was subjected to various cooking and acid or alkali treatments in order to improve the digestibility of pea protein for use in calf milk replacers. Treatment effects were assessed by in vitro digestion with rennin, pepsin and calf abomasal fluids. Oven heating at 95–246 C for 5 min to 15 h or steam heating at 1.06 kg/cm2 for 4 h failed to improve digestibility. Treatment of PPC in an aqueous medium at pH values from 2 to 12 for 5 h at 37 C resulted in higher digestibility. A pH of 2.0 or 10.6 was most effective. Acid or alkali hydrolysis of PPC at 110 C for 4–5 h increased digestibility, but adversely affected amino acid content. Rennin was consistently less effective than pepsin or abomasal contents in digesting PPC. The pH of abomasal contents from young calves fed milk replacers may be too high for effective pepsin activity. These factors could account for the low digestibility of non-milk proteins by calves under 2 wk of age.

Download Full-text

Hydrolysis of peanut (Arachis hypogea L) protein concentrate by fungal crude protease extract: effect on structural, functional and in-vitro protein digestibility

Journal of Food Science and Technology ◽

10.1007/s13197-021-05225-y ◽

2021 ◽

Author(s):

Deep Narayan Yadav ◽

Nisar Ahmad Mir ◽

Ritika Wadhwa ◽

Surya Tushir ◽

Swati Sethi ◽

...

Keyword(s):

Protein Digestibility ◽

Protein Concentrate ◽

In Vitro Protein Digestibility ◽

L Protein ◽

Arachis Hypogea ◽

Hydrolysis Of ◽

Vitro Protein

Download Full-text

Digestion of soybean globulins, glycinin, α-conglycinin and β-conglycinin in the preruminant and the ruminant calf

Canadian Journal of Animal Science ◽

10.4141/cjas93-091 ◽

1993 ◽

Vol 73 (4) ◽

pp. 891-905 ◽

Cited By ~ 21

Author(s):

H. M. Tukur ◽

J. P. Lallès ◽

C. Mathis ◽

I. Caugant ◽

R. Toullec

Keyword(s):

Key Words ◽

Soybean Protein ◽

Point Of View ◽

Protein Concentrate ◽

Protein Digestion ◽

Soybean Globulins ◽

Milk Replacers ◽

Meal Product

Two experiments involving either preruminant (exp. 1) or ruminant (exp. 2) fistulated calves were conducted to study the in vivo digestion of glycinin, α-conglycinin and β-conglycinin from soybean. It was incorporated as a flour (product A, antigenic in vitro) or a protein concentrate (product B, non antigenic in vitro) in milk replacers (exp. 1), or as a meal (product C, antigenic in vitro) in a weaning starter (exp. 2). ELISA detection of residual globulin immunoreactivity was determined on ileal digesta in exp. 1, and on duodenal, ileal and faecal digesta in exp. 2. Ileal flow of glycinin, α-conglycinin and β-conglycinin represented 10.3, 1.2 and 0.9% of corresponding globulin amounts ingested, in the case of product A (exp. 1). Immunoreactive α-conglycinin could only be detected in ileal digesta (1.3% of intake) of calves fed the diet containing product B. In exp. 2, immunoreactive globulins entered the duodenum in low amounts (below 1% of respective intake), especially after weaning. Accordingly, their flow at the ileum and in feces, although measurable, had no meaning from the nutritional point of view. Fermentation in the rumen of weaned calves appeared to be efficient in inactivating most of the potentially harmful dietary constituents. Key words: Soybean, protein, digestion, calf, weaning, glycinin

Download Full-text

SUSCEPTIBILITY OF PROTEINS USED IN CALF MILK REPLACERS TO HYDROLYSIS BY VARIOUS PROTEOLYTIC ENZYMES

Canadian Journal of Animal Science ◽

10.4141/cjas80-106 ◽

1980 ◽

Vol 60 (4) ◽

pp. 907-914 ◽

Cited By ~ 17

Author(s):

K. J. JENKINS ◽

S. MAHADEVAN ◽

D. B. EMMONS

Keyword(s):

Trichloroacetic Acid ◽

Proteolytic Enzymes ◽

Milk Proteins ◽

In Vitro Study ◽

Enzyme Treatment ◽

Protein Hydrolysis ◽

Protein Substrates ◽

Optimum Ph ◽

Milk Replacers

An in vitro study was conducted to assess the hydrolytic susceptibility of various milk and non-milk proteins (soybean, rapeseed, fish) used in calf milk replacers to endogenous and commercial proteolytic enzymes. Extent of protein hydrolysis (%) was calculated from the reduced amount of protein precipitated by 10% trichloroacetic acid following enzyme treatment. All of the enzymes tested hydrolyzed the milk proteins more extensively than the non-milk proteins both at their optimum pH, and at the pH (6.1) of calf abomasal contents immediately after feeding. At both optimum pH and pH 6.1, the highest average hydrolysis value for all protein substrates was obtained with pronase followed by papain, trypsin, pancreatin, chymotrypsin, Mucor miehei rennet andchymosin (calf rennet). All substrates were hydrolyzed extensively by pepsin at pH 2.0 but, as expected, very little hydrolysis occurred with this enzyme atpH6.1.

Download Full-text

REDUCTION OF β-CONGLYCININ ANTIGENICITY AND RATE OF ACID-PEPSIN PROTEOLYSIS OF PROTEINS IN EXTRUDED OR RUMEN FLUID-TREATED SOYBEAN MEAL

Canadian Journal of Animal Science ◽

10.4141/cjas89-085 ◽

1989 ◽

Vol 69 (3) ◽

pp. 727-734 ◽

Cited By ~ 3

Author(s):

P. S. MIR ◽

J. H. BURTON ◽

B. N. WILKIE ◽

F. R. VAN DE VOORT

Keyword(s):

Soybean Meal ◽

Rumen Fluid ◽

Milk Powder ◽

Skim Milk ◽

In Vitro Digestion ◽

Skim Milk Powder ◽

Negative Control ◽

Fermented Soybean Meal ◽

Milk Replacers

The effect of processing commercial soybean meal (HSBM) by either extrusion (ExSBM) or fermentation with microbes in rumen fluid (FSBM) on rate of protein hydrolysis and the activity of the antigen β-conglycinin was evaluated. Ethanol-extracted soybean meal (EtSBM) and skim milk powder (SMP) were included as positive controls while HSBM was the negative control, with regard to antigen content. The rates of proteolysis were determined by acid pepsin hydrolysis and the activity of β-conglycinin in the soluble fraction of the digestion mixtures at 0, 2, 4, 6 and 8 h of in vitro proteolysis was determined by radial immunodiffusion in agar gel containing antibody specific for the antigen. Susceptibility of FSBM and ExSBM to proteolysis by pepsin was greater than that of EtSBM. β-Conglycinin content was greatest in HSBM (1.0 ± 0.2 g dL−1) and only 0.3 ± 0.03 g dL−1 in ExSBM at the beginning of in vitro digestion. The antigen was not detected in either FSBM or EtSBM, therefore these products could be used in milk replacers for calves. Key words: In vitro pepsin proteolysis, extruded soybean meal, fermented soybean meal, antigen, β-conglycinin

Download Full-text

Transport across Caco-2 monolayers of peptides arising from in vitro digestion of bovine milk proteins

Food Chemistry ◽

10.1016/j.foodchem.2013.01.063 ◽

2013 ◽

Vol 139 (1-4) ◽

pp. 203-212 ◽

Cited By ~ 65

Author(s):

Gianluca Picariello ◽

Giuseppe Iacomino ◽

Gianfranco Mamone ◽

Pasquale Ferranti ◽

Olga Fierro ◽

...

Keyword(s):

Bovine Milk ◽

Milk Proteins ◽

In Vitro Digestion ◽

Bovine Milk Proteins

Download Full-text

Impact of Acetic Acid on the Survival ofL. plantarumupon Microencapsulation by Coaxial Electrospraying

Journal of Healthcare Engineering ◽

10.1155/2017/4698079 ◽

2017 ◽

Vol 2017 ◽

pp. 1-6 ◽

Cited By ~ 6

Author(s):

Laura G. Gómez-Mascaraque ◽

Jesús Ambrosio-Martín ◽

Rocío Perez-Masiá ◽

Amparo Lopez-Rubio

Keyword(s):

Acetic Acid ◽

Inner Core ◽

In Vitro Digestion ◽

Probiotic Bacteria ◽

Whey Protein Concentrate ◽

Protein Concentrate ◽

Outer Solution ◽

Protein Particles ◽

First Time

In this work, coaxial electrospraying was used for the first time to microencapsulate probiotic bacteria, specificallyLactobacillus plantarum, within edible protein particles with the aim of improving their resistance to in vitro digestion. The developed structures, based on an inner core of whey protein concentrate and an outer layer of gelatin, were obtained in the presence of acetic acid in the outer solution as a requirement for the electrospraying of gelatin. Despite the limited contact of the inner suspension and outer solution during electrospraying, the combination of the high voltage used during electrospraying with the presence of acetic acid was found to have a severe impact on the lactobacilli, not only decreasing initial viability but also negatively affecting the survival of the bacteria during storage and their resistance to different stress conditions, including simulated in vitro digestion.

Download Full-text