ASSESSMENT OF HEAT DAMAGE TO PROTEIN DIGESTIBILITY FROM FISH MEALS BY IN VITRO PEPSIN SOLUBILIZATION AT DIFFERENT TEMPERATURES

1982 ◽  
Vol 62 (2) ◽  
pp. 657-660 ◽  
Author(s):  
B. E. MARCH ◽  
D. R. HICKLING
Keyword(s):  
Standard Method ◽  
Fish Meal ◽  
Cold Water ◽  
Protein Digestibility ◽  
In Vitro Digestion ◽  
Control Fish ◽  
Pepsin Digestion ◽  
Water Fish ◽  
Different Temperatures

A control fish meal and an overheated fish meal were compared by in vitro digestion with pepsin at concentrations of 10−5 to 10−1 and at temperatures from 10 to 40 °C. The reduction in protein solubilization caused by over-heating was most evident with pepsin digestion at 10 and 20 °C and suggests modification of the standard method when evaluating fish meals to be fed to cold-water fish. Key words: Protein digestibility, pepsin digestibility, fish meal, cold-water fish

scholarly journals Nutritional quality and in vitro digestion of immature rice-based processed products

2020 ◽  
Vol 11 (9) ◽  
pp. 7611-7625
Author(s):  
Kulwa F. Miraji ◽  
Anita R. Linnemann ◽  
Vincenzo Fogliano ◽  
Henry S. Laswai ◽  
Edoardo Capuano
Keyword(s):  
Nutritional Quality ◽  
Protein Digestibility ◽  
In Vitro Digestion ◽  
Nutritional Properties ◽  
Processed Products

The nutritional contents of rice decreased as grains matured, and pepeta-type processing improves the nutritional properties and in vitro protein digestibility of rice.

scholarly journals The effects of environmental temperature on the properties of myofibrillar adenosine triphosphatase from various species of fish

1973 ◽  
Vol 133 (4) ◽  
pp. 735-738 ◽  
Author(s):  
Ian A. Johnston ◽  
Neil Frearson ◽  
Geoffrey Goldspink
Keyword(s):  
Low Temperatures ◽  
Half Life ◽  
Adenosine Triphosphatase ◽  
Environmental Temperature ◽  
Cold Water ◽  
Warm Water ◽  
Adenosine Triphosphatase Activity ◽  
Water Fish ◽  
Different Temperatures ◽  
Myotomal Muscle

1. Myofibrillar adenosine triphosphatase (ATPase) activities were measured for white myotomal muscle of 19 species of fish. 2. The activity was measured at different temperatures and after periods of preincubation at 37°C. 3. The inactivation half-life at 37°C depended on environmental temperature, increasing as the temperature increased. 4. Cold-water fish had higher myofibrillar adenosine triphosphatase activity at low temperatures than had warm-water fish. 5. The significance of these results is discussed.

scholarly journals Scientific Background of Dairy Protein Digestibility: A Review

2014 ◽  
Vol 7 ◽  
pp. 1-8 ◽  
Author(s):  
Ashok Kumar Shrestha
Keyword(s):  
Amino Acids ◽  
Whey Proteins ◽  
Protein Digestibility ◽  
In Vitro Digestion ◽  
Dairy Proteins ◽  
Dairy Foods ◽  
Dairy Protein ◽  
Protein Rich ◽  
And Control

Recent advances have shown that differences in compositional, structural and physical properties of caseins and whey proteins affect their digestion and absorption behavior, hormonal response, satiety effect and other physiological effects. For example, the ingestion of whey protein cause fast, high and transient increase of amino acids ‘fast protein’, whereas casein induce slower, lower and prolonged increase of ‘slow protein’ in the gut. Knowledge of, and control over, the rate and nature of digestive breakdown of dairy proteins provides a potential basis for product/process innovation through identifying ingredients and formulations that provide desired nutrient delivery profiles. With this background, the aim of our current review paper is to understand the digestion behavior of various protein-rich milk powders and their potential use in formulation of dairy foods for controlled release of amino acids and energy. Currently available in vitro protein digestibility methods to measure or predict the dairy protein digestibility were also investigated. The author has also presented the preliminary results of ongoing study on in vitro digestion of various commercial proteins powders.DOI: http://dx.doi.org/10.3126/jfstn.v7i0.10560 J. Food Sci. Technol. Nepal, Vol. 7 (1-8), 2012

Effect of Pepsin Treatment on the Chemical Iron Profile of Soy-Based Foods Supplemented with Selected Iron Sources and Enhancers

1985 ◽  
Vol 48 (1) ◽  
pp. 35-38 ◽  
Author(s):  
S.W. RIZK ◽  
F.M. CLYDESDALE
Keyword(s):  
Ascorbic Acid ◽  
Citric Acid ◽  
Degradation Products ◽  
In Vitro Digestion ◽  
Soy Milk ◽  
Pepsin Digestion ◽  
Iron Solubility ◽  
Iron Profile ◽  
Solubilizing Capacity

Changes in chemical iron profile occurring from pH 2 to 6.5 in a wheat-soy blend, a corn-soy-milk mix, and a soy-extended beef patty were investigated. Iron solubility in these products, as affected by in vitro digestion with pepsin, was dependent on a combination of ligand, iron source, pH and food. The greatest solubilizing capacity of the ligands added was provided by ascorbic acid at pH 2 and 4, and by citric acid at pH 6. Improvements in percent soluble iron were related to pepsin digestion and the presumed appearance of protein degradation products.

Increased protein digestibility of beef with aging in an infant in vitro digestion model

Meat Science ◽  
2020 ◽  
Vol 169 ◽  
pp. 108210 ◽  
Author(s):  
Seonmin Lee ◽  
Kyung Jo ◽  
Hyun Jung Lee ◽  
Cheorun Jo ◽  
Hae In Yong ◽  
...  
Keyword(s):  
Protein Digestibility ◽  
In Vitro Digestion

Role of the bolus degree of structure on the protein digestibility during in vitro digestion of a pea protein‐fortified sponge cake chewed by elderly

2019 ◽  
Author(s):  
Melissa Assad‐Bustillos ◽  
Juliette Palier ◽  
Hanitra Rabesona ◽  
Yvan Choiset ◽  
Guy Della Valle ◽  
...  
Keyword(s):  
Protein Digestibility ◽  
In Vitro Digestion ◽  
Pea Protein ◽  
Sponge Cake

Determination of protein digestibility of animal protein feeds under condition of in vitro and in vivo

2007 ◽  
Vol 2007 ◽  
pp. 27-27
Author(s):  
Abolfazl Zarei ◽  
Ahmad Mirhadi ◽  
Mahmood Shivazad ◽  
Hoshang Lotfollahian
Keyword(s):  
Fish Meal ◽  
High Salinity ◽  
Protein Digestibility ◽  
Good Source ◽  
Tropical Regions ◽  
Poultry Diets ◽  
Different Sources

Artemia or brine shrimp is a crustacean animal that lives in conditions of high salinity in the tropical and sub-tropical regions of the world. There is great potential for the culture and production of artemia in Iran. Artemia biomass is a good source of protein that can be used in poultry diets (Zarei et al., 2006). The objective of this study was to determine the protein digestibility of different sources of artemia in vitro and in vivo in comparison with fish meal.

In vitro digestion rate and resistant starch content of tortillas stored at two different temperatures

LWT ◽  
2006 ◽  
Vol 39 (8) ◽  
pp. 947-951 ◽  
Author(s):  
José Juan Islas-Hernández ◽  
Rodolfo Rendón-Villalobos ◽  
Edith Agama-Acevedo ◽  
Felipe Gutiérrez-Meraz ◽  
Juscelino Tovar ◽  
...  
Keyword(s):  
Resistant Starch ◽  
Starch Content ◽  
In Vitro Digestion ◽  
Digestion Rate ◽  
Different Temperatures

scholarly journals Soy Protein Pressed Gels: Gelation Mechanism Affects the In Vitro Proteolysis and Bioaccessibility of Added Phenolic Acids

Foods ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 154
Author(s):  
Marina Marinea ◽  
Ashling Ellis ◽  
Matt Golding ◽  
Simon M. Loveday
Keyword(s):  
Amino Acid ◽  
Phenolic Acids ◽  
Soy Protein ◽  
Protein Digestibility ◽  
In Vitro Digestion ◽  
Delivery Systems ◽  
Gelation Mechanism ◽  
Coagulation Mechanism ◽  
Percentage Basis

In this study, a model system of firm tofu (pressed gel) was prepared to study how the coagulation mechanism—acidification with glucono δ-lactone (GDL) or coagulation with magnesium sulphate (MgSO4)—affected the physical properties of the gels along with their in vitro proteolysis (or extent of proteolysis). The two types of gels were also fortified with 3.5 mM protocatechuic (PCA) and coumaric acid (CMA) to test whether they can be used as bioactive delivery systems. Texture analysis showed that all MgSO4-induced gels (fortified and control) had a higher hydration capacity and a weaker texture than the GDL-induced gels (p < 0.05). MgSO4 gels had almost double proteolysis percentages throughout the in vitro digestion and showed a significantly higher amino acid bioaccessibility than the GDL gels (essential amino acid bioaccessibility of 56% versus 31%; p < 0.05). Lastly, both gel matrices showed a similar phenolic acid release profile, on a percentage basis (~80% for PCA and ~100% for CMA). However, GDL gels delivered significantly higher masses of bioactives under simulated intestinal conditions because they could retain more of the bioactives in the gel after pressing. It was concluded that the coagulation mechanism affects both the macro- and microstructure of the soy protein pressed gels and as a result their protein digestibility. Both pressed gel matrices are promising delivery systems for bioactive phenolic acids.

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