scholarly journals In vitro Determination of the Release Kinetics of Peptides and Free Amino Acids During the Digestion of Food Proteins

2005 ◽  
Vol 88 (3) ◽  
pp. 935-948 ◽  
Author(s):  
Laurent Savoie ◽  
Rafael A Agudelo ◽  
Sylvie F Gauthier ◽  
Johanne Marin ◽  
Yves Pouliot
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Protein Quality ◽  
Release Kinetics ◽  
In Vitro Digestion ◽  
Exchange Chromatography ◽  
Protein Sources ◽  
Kinetics Of ◽  
Peptide Fractions

Abstract The kinetics of peptide release during in vitro digestion of 4 protein sources (casein, cod protein, soy protein, and gluten) were investigated. Samples were sequentially hydrolyzed with pepsin (30 min) and pancreatin (2, 4, or 6 h) in a dialysis cell with continuous removal of digestion products. Nondialyzed digests were fractionated by ion-exchange chromatography and ultrafiltration. Animal proteins were digested at a greater rate than plant proteins. Target amino acids of specific enzymes appeared more rapidly in the dialyzed fractions when compared to other amino acids. Throughout the hydrolysis, nondialyzed digests contained a higher proportion of peptide mixtures with basic-neutral properties. Except for gluten, peptide fractions with molecular weights that exceeded 10 kDa (basic-neutral, BN > 10) were rapidly hydrolyzed during the first 2 h of pancreatin digestion. The kinetics of release and the composition of peptide fractions were different when the protein sources were compared. The analysis of amino acids revealed that threonine and proline proportions were relatively high in BN > 10 and in peptide fractions with molecular weight between 10-1 kDa (BN 10-1), while tyrosine, phenylalanine, lysine, and arginine predominated in the low molecular weight (<1 kDa) fractions. More resistant peptides were generally rich in proline and glutamic acid. The role of in vitro digestion assays in dietary protein quality evaluation is discussed.

scholarly journals Impact of exocrine pancreatic adaptation on in vitro protein digestibility

1993 ◽  
Vol 69 (2) ◽  
pp. 359-369 ◽  
Author(s):  
P. Valette ◽  
H. Malouin ◽  
T. Corring ◽  
L. Savoie
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Pancreatic Enzyme ◽  
Protein Digestibility ◽  
Low Molecular Weight ◽  
Rapeseed Proteins ◽  
Total Capacity ◽  
Kinetics Of

An in vitro enzymic method was used to study the kinetics of digestion of casein and rapeseed proteins. After a predigestion step with pepsin (EC 3.4.23.1), the protein substrates were submitted to a 24 h hydrolysis either with pancreatin or pancreatic juices of pigs adapted either to casein or rapeseed diets and whose enzyme activities were different. After 3, 6 and 24 h of in vitro digestion, dialysates were collected and analysed for content of nitrogen, amino acids and low-molecular-weight peptides. For a long-term hydrolysis (24 h), overall digestibility of both substrates was not affected by the composition of pancreatic enzyme mixtures. However, at the beginning of hydrolysis a significant effect of pancreatic juices was observed, i.e. individual amino acid digestibility was generally higher when casein pancreatic juice was used for hydrolysis and their relative pattern of release was modified. For both substrates the proportion of amino acids released as low-molecular-weight peptides was not affected by the enzyme mixture used and made up about two-thirds of the total digested material. It is concluded that exocrine pancreatic adaptation to protein sources does not affect the total capacity of protein digestion. However, the changes in initial kinetics of release of amino acids are more dependent on the nature of the protein tested than on the composition of pancreatic enzyme mixtures.

scholarly journals Effect of Molecular Weight of Tilapia (Oreochromis Niloticus) Skin Collagen Peptide Fractions on Zinc-Chelating Capacity and Bioaccessibility of the Zinc-Peptide Fractions Complexes in Vitro Digestion

2020 ◽  
Vol 10 (6) ◽  
pp. 2041
Author(s):  
Lei Chen ◽  
Xuanri Shen ◽  
Guanghua Xia
Keyword(s):  
Molecular Weight ◽  
In Vitro Digestion ◽  
Zinc Complexes ◽  
Low Molecular Weight ◽  
Collagen Peptide ◽  
Skin Collagen ◽  
Chelating Ability ◽  
Zinc Chelation ◽  
Peptide Fractions

To investigate the effect of the molecular weight of tilapia skin collagen peptide fractions on their zinc chelation capacity and the bioaccessibility of their zinc complexes, we evaluated the zinc-chelating ability of different molecular weight peptide, the solubility, and the stability of the complexes during simulated in vitro digestion. Low molecular weight peptide (P1) exhibited a higher zinc-chelating ability, which can be attributed to the variety of metal chelate amino acid residues. The highest solubility and the lowest release of zinc during peptic digestion for the P1-zinc complex and the zinc binding to P1 were retained at approximately 50% after peptic-pancreatic digestion. Fourier transform infrared spectroscopy indicated the primary involvement of the N-H group in all peptide-zinc complexes. This finding suggests that low molecular weight peptidefraction with strong zinc chelation ability can be used as delivery agents to improve zinc bioaccessibility.

scholarly journals Identification in skeletal muscle of a distinct extracellular pool of amino acids, and its role in protein synthesis

1971 ◽  
Vol 121 (5) ◽  
pp. 817-827 ◽  
Author(s):  
R. C. Hider ◽  
E. B. Fern ◽  
D. R. London
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Incubation Medium ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Longus Muscle ◽  
Kinetics Of

1. The kinetics of radioactive labelling of extra- and intra-cellular amino acid pools and protein of the extensor digitorum longus muscle were studied after incubations with radioactive amino acids in vitro. 2. The results indicated that an extracellular pool could be defined, the contents of which were different from those of the incubation medium. 3. It was concluded that amino acids from the extracellular pool, as defined in this study, were incorporated directly into protein.

In vitro digestion of protein sources by crude enzyme extracts of the spiny lobster Panulirus argus (Latreille, 1804) hepatopancreas with different trypsin isoenzyme patterns

Aquaculture ◽  
2010 ◽  
Vol 310 (1-2) ◽  
pp. 178-185 ◽  
Author(s):  
Erick Perera ◽  
F.J. Moyano ◽  
L. Rodriguez-Viera ◽  
A. Cervantes ◽  
G. Martínez-Rodríguez ◽  
...  
Keyword(s):  
Spiny Lobster ◽  
In Vitro Digestion ◽  
Crude Enzyme ◽  
Panulirus Argus ◽  
Protein Sources ◽  
Isoenzyme Patterns

Fabrication and Release Kinetics of Liposomes Containing Leuprolide Acetate

2021 ◽  
Vol 7 (1) ◽  
pp. 35-38
Author(s):  
Sudipta Das ◽  
Arnab Samanta ◽  
Koushik Bankura ◽  
Debatri Roy ◽  
Amit Nayak
Keyword(s):  
Drug Release ◽  
Release Kinetics ◽  
In Vitro Release ◽  
Zero Order ◽  
Leuprolide Acetate ◽  
Lipid Film ◽  
In Vitro Drug Release ◽  
Liposomal Formulations ◽  
Kinetics Of

The present work is focused on the preparation and in vitro release kinetics of liposomal formulation of Leuprolide Acetate. In this work, “Thin Lipid Film Hydration Method” was used for preparation of Leuprolide Acetate loaded liposomes. Prepared liposomal formulations of Leuprolide acetate was evaluated by drug entrapment study, in-vitro drug release kinetics and stability studies. The percentage drug entrapment of Leuprolide acetate for F1 and F2 formulations were found to be 78.14 ± 0.67 and 66.70 ± 0.81% respectively. In-vitro drug release study of liposomal formulations had shown zero order release pattern. Regression co-efficient (R2) value of Zero order kinetics for F1 and F2 formulations were 0.9912 and 0.9676 respectively. After storing formulations for 1 month, stability testing was done at 40C.It was found that all batches were stable. These liposomal formulations of Leuprolide acetate can be formulated for parenteral application to treat prostate cancer and in women, to treat symptoms of endometriosis (overgrowth of uterine lining outside of the uterus) or uterine fibroids.

scholarly journals In vitro protein digestion kinetics of protein sources for pigs

animal ◽  
2019 ◽  
Vol 13 (6) ◽  
pp. 1154-1164 ◽  
Author(s):  
H. Chen ◽  
P.A. Wierenga ◽  
W.H. Hendriks ◽  
A.J.M. Jansman
Keyword(s):  
Protein Digestion ◽  
Protein Sources ◽  
Digestion Kinetics ◽  
Kinetics Of ◽  
Vitro Protein

FACTORS INFLUENCING THE NUTRITIONAL VALUE OF FISH FLOUR: III. FURTHER STUDIES ON AVAILABILITY OF AMINO ACIDS

1963 ◽  
Vol 41 (7) ◽  
pp. 1589-1594 ◽  
Author(s):  
A. B. Morrison
Keyword(s):  
Amino Acids ◽  
Nutritional Value ◽  
Chloride Content ◽  
In Vitro Digestion ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Deficient Diet ◽  
Weight Gains ◽  
Flour Sample

Weight gains of male weanling rats given fish flour sample X were significantly increased by addition to the diet of methionine, histidine, threonine, and tryptophan. When histidine or methionine were omitted from the amino acid mixture, weight gains were similar to those found with the unsupplemented flour, and the combination of methionine and histidine was as effective as the four amino acids. Supplements of histidine and methionine had no effect on weight gains of rats given fish flour sample CFF, which was of high nutritional value. Sample X contained methionine in an amount similar to that of sample CFF, and somewhat less histidine. The amounts of methionine and histidine released during in vitro digestion with pancreatin were much less for sample X than for sample CFF. Steaming sample X for 30 minutes significantly increased its gross protein value determined in a methionine-deficient diet, but had no effect on the total or organic chloride content. It was concluded that sample X contained unavailable methionine and histidine.

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