Influence of Feeding Alkaline/Heat Processed Proteins on Growth and Protein and Mineral Status of Rats

Sarwar, Ghulam; L’Abbé, Mary R.; Trick, Keith D.; Botting, H. G.; Y., C.

doi:10.1007/978-1-4615-4853-9_11

Cited by 23 publications

(25 citation statements)

References 20 publications

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“…Heating at 65 °C for 24 hours at pH 10.5–11.5 caused LAL formation and racemization, resulting in 13–18% decreases in ileal digestibility for casein, β-lactoglobulin and wheat proteins in minipigs (Vrese et al, 2000). Digestibility of alkali and heat-treated caseins and soy proteins is also reduced in rats (Sarwar et al, 1999). …”

Section: Processing Techniques Alter Protein Digestibilitymentioning

confidence: 99%

Personalizing protein nourishment

Dallas

Sanctuary

et al. 2017

Critical Reviews in Food Science and Nutrition

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Proteins are not equally digestible—their proteolytic susceptibility varies by their source and processing method. Incomplete digestion increases colonic microbial protein fermentation (putrefaction), which produces toxic metabolites that can induce inflammation in vitro and have been associated with inflammation in vivo. Individual humans differ in protein digestive capacity based on phenotypes, particularly disease states. To avoid putrefaction-induced intestinal inflammation, protein sources and processing methods must be tailored to the consumer’s digestive capacity. This review explores how food processing techniques alter protein digestibility and examines how physiological conditions alter digestive capacity. Possible solutions to improving digestive function or matching low digestive capacity with more digestible protein sources are explored. Beyond the ileal digestibility measurements of protein digestibility, less invasive, quicker and cheaper techniques for monitoring the extent of protein digestion and fermentation are needed to personalize protein nourishment. Biomarkers of protein digestive capacity and efficiency can be identified with the toolsets of peptidomics, metabolomics, microbial sequencing and multiplexed protein analysis of fecal and urine samples. By monitoring individual protein digestive function, the protein component of diets can be tailored via protein source and processing selection to match individual needs to minimize colonic putrefaction and, thus, optimize gut health.

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Section: Processing Techniques Alter Protein Digestibilitymentioning

confidence: 99%

Personalizing protein nourishment

Dallas

Sanctuary

et al. 2017

Critical Reviews in Food Science and Nutrition

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“…As a consequence, the results are contrasting: on one hand the soy protein hydrolysates increase Ca uptake in the CaCO 2 cells [14], on the other hand LAL production decreases the digestibility of the protein and mineral fractions [15,16]. Brink et al [10] found less Ca digestibility in soya milk than in cow's milk, which confirms the lower level of absorption of this mineral in soya than in milk.…”

Section: In Vivo Ca Digestibilitymentioning

confidence: 79%

In vivo and in vitro digestibility of the calcium contained in foods of animal and plant origin

Eugenia

Bruschi

Mulazzi

et al. 2010

Mediterr J Nutr Metab

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The aim of this study was to assess Ca digestibility using in vitro and in vivo methodology (rats).The tested foods were: cheese (Grana Padano; Emmentaler), soybean-based products (tofu; burger; milk; yogurt), and legumes (peas; beans). Ca digestibility was found to be high in Emmentaler (84.3%), Grana Padano (83.6%) and tofu (80.3%), with significantly lower values for soya burgers (64.1%) and soya milk (60.6%). The lowest values were detected in peas (49.6%) and beans (31.4%). Poor correlation was found between in vivo and in vitro data. The current RDAs have been established on the basis of 30% Ca digestibility, a value which reduces the risk of calcium deficiency but underestimates the contribution of dairy products. The adoption of specific, instead of general, digestibility values for each food might improve the accuracy of dietary formulations. This will require considerable efforts to develop simple and reliable in vitro methods to assess foods.

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“…The BUN test is a measurement of the amount of nitrogen in the blood in the form of urea, and BUN values are affected by dietary protein. 15) The BUN values of the control rats were slightly lower than the normal range of BUN values for SD rats, and the BUN values of the rats treated with yeast hydrolysate with below 10 kDa molecular weight, which is a rich source of protein and Values are means ± S.D. for 5 rats/group.…”

Section: Hematological and Biochemical Parametersmentioning

confidence: 86%

Safety Study of Yeast Hydrolysate with below 10 kDa Molecular Weight in Animal Models

Jung

Park

Kim

et al. 2011

JOURNAL OF HEALTH SCIENCE

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The aim of this study was to obtain data on the safety of yeast hydrolysate with below 10 kDa molecular weight. The acute [at a single dose of 5000 mg/kg body weight (BW)] and subacute (at a dose of 1000 mg/kg BW for 14 consecutive days) oral toxicity of yeast hydrolysate from Saccharomyces cerevisiae was assessed in Sprague-Dawley (SD) rats. The yeast hydrolysate acute treatment via the oral route at the dose of up to 5000 mg/kg did not produce any signs of toxicity or death in the rats. The yeast hydrolysate with below 10 kDa molecular weight did not induce any damage to the internal organs of the rats as examined by hematological and biochemical parameters. The macroscopic analysis of the treated animals did not show significant changes in color and texture. These results show that yeast hydrolysate with below 10 kDa molecular weight possesses very low toxicity as indicated in this SD rat model.

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Influence of Feeding Alkaline/Heat Processed Proteins on Growth and Protein and Mineral Status of Rats

Cited by 23 publications

References 20 publications

Personalizing protein nourishment

Personalizing protein nourishment

In vivo and in vitro digestibility of the calcium contained in foods of animal and plant origin

Safety Study of Yeast Hydrolysate with below 10 kDa Molecular Weight in Animal Models

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