Molecular weight determination of hydrolyzed collagens

Denis, Alain; Brambati, Noëlle; Dessauvages, Bernadette; Guedj, Sylviane; Ridoux, Claude; Meffre, Nicole; Autier, Claude

doi:10.1016/j.foodhyd.2007.05.016

Cited by 40 publications

(32 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The use of formol titration for assessing the degree of hydrolysis is based on the fact that the reaction of the sample with formaldehyde releases a proton (H + ) from the free amino group that can be titrated with an alkaline solution. Thereafter, the amount of alkali added, after subtraction of the blank value, is considered to be equivalent to the amount of α -amino groups present in the protein solution (Denis et al 2008). However, the release of certain amino acids with titrated side chains and the buffering capacity of the amino groups might interfere with this titration (Levy 1935).…”

Section: Resultsmentioning

confidence: 99%

Action of a pancreatin and an Aspergillus oryzae protease on whey proteins: correlation among the methods of analysis of the enzymatic hydrolysates

Morais

Silvestre

Silveira

et al. 2013

Braz. arch. biol. technol.

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 99%

Action of a pancreatin and an Aspergillus oryzae protease on whey proteins: correlation among the methods of analysis of the enzymatic hydrolysates

Morais

Silvestre

Silveira

et al. 2013

Braz. arch. biol. technol.

View full text Add to dashboard Cite

show abstract

“…HC is usually presented as a white powder with good solubilisation properties, commonly used as a dietary supplement or included in various foodstuffs. Like for gelatin, HC molecular weight distribution, structure and composition, and subsequently functional properties, depend on the processing conditions as well as the raw material and the specificity of the enzyme used to hydrolyze the gelatin (Denis et al, 2008). The average molecular weight of HC ranges between 2,000 and 6,000 Daltons (Moskowitz, 2000).…”

Section: Collagen In Nutrition and Food Supplementsmentioning

confidence: 99%

Biological Effect of Hydrolyzed Collagen on Bone Metabolism

Daneault

Coxam

Wittrant

2015

Critical Reviews in Food Science and Nutrition

View full text Add to dashboard Cite

Osteoporosis is a chronic and asymptomatic disease characterized by low bone mass and skeletal microarchitectural deterioration, increased risk of fracture, and associated comorbidities most prevalent in the elderly. Due to an increasingly aging population, osteoporosis has become a major health issue requiring innovative disease management. Proteins are important for bone by providing building blocks and by exerting specific regulatory function. This is why adequate protein intake plays a considerable role in both bone development and bone maintenance. More specifically, since an increase in the overall metabolism of collagen can lead to severe dysfunctions and a more fragile bone matrix and because orally administered collagen can be digested in the gut, cross the intestinal barrier, enter the circulation, and become available for metabolic processes in the target tissues, one may speculate that a collagen-enriched diet provides benefits for the skeleton. Collagen-derived products such as gelatin or hydrolyzed collagen (HC) are well acknowledged for their safety from a nutritional point of view; however, what is their impact on bone biology? In this manuscript, we critically review the evidence from literature for an effect of HC on bone tissues in order to determine whether HC may represent a relevant alternative in the design of future nutritional approaches to manage osteoporosis prevention.

show abstract

“…The collagen hydrolysate provides great potential for use in preparations for skin care and hair care, in solid dosage forms of drugs and in numerous foods since they can be easily mixed with other products without causing alteration of the sensory properties of the product (DENIS et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Profiles of Enzymatic Hydrolysis of Different Collagens and Derivatives Over Time

Iltchenco¹,

Kempka

Prestes³

2017

R. bras. Tecnol. Agroindustr.

View full text Add to dashboard Cite

The interest in collagen use in the food industry to replace synthetic agents is growing every day. Among the derivatives, has the hydrolysate, which dissolves easily in water and brine, and can be incorporated into foods or drinks. The objective of this study was to determine the degree of hydrolysis (DH) of crude collagen fiber, powdered collagen fiber, gelatin and two samples of hydrolyzed collagen. The substrates were subjected to individual action of three proteolytic enzymes: papain, bromelain and collagenase (microbial origin). The substrates were incubated in sodium phosphate buffer (0.1 M, pH 7.0) on an orbital shaker at 55 °C for different periods of time. In 120 minutes of hydrolysis, the crude collagen fiber showed 37.2% of DH using collagenase, the highest value compared to other substrates. The lowest values for DH were obtained for the hydrolysates collagen, with less than 1 % of DH. For hydrolysis in 60 minutes, the DH values were similar to those obtained in 120 minutes of hydrolysis, with minor variations over time. The hydrolytic ability of the collagenase and bromelain was similar and superior compared with the papain.

show abstract

Molecular weight determination of hydrolyzed collagens

Cited by 40 publications

References 25 publications

Action of a pancreatin and an Aspergillus oryzae protease on whey proteins: correlation among the methods of analysis of the enzymatic hydrolysates

Action of a pancreatin and an Aspergillus oryzae protease on whey proteins: correlation among the methods of analysis of the enzymatic hydrolysates

Biological Effect of Hydrolyzed Collagen on Bone Metabolism

Profiles of Enzymatic Hydrolysis of Different Collagens and Derivatives Over Time

Contact Info

Product

Resources

About