The comparative inference of antidiabetic status of hydrolysates raw and boiled with reference to different incubation periods was tabulated Table Among the three different enzymes, hydrolysates treated with chymotrypsin shows highest antidiabetic activity than hydrolysates obtained with trypsin and pepsin enzymes.
Overall, raw milk casein hydrolysates always showed the higher antidiabetic effect as compared to boiled milk casein hydrolysates, irrespective of the enzyme used Figure Casein prepared isoelectrically was treated with three different enzymes so as to break the caseinates into peptides having desired biological activities.
These peptides obtained after hydrolysis were further analyzed for extend of hydrolysis. The DH was estimated by quantifying the undigested protein as well as measuring the content of peptide bonds cleaved during different enzymatic treatments. The increase in the released amino acids relates to the increase in the DH.
The decrease in the DH after boiling may be due to the denaturation of milk casein due to which the respective enzymes fails to recognize their specific binding sites and thereby unable to cleave its specific structural motifs. Denaturation hampers enzyme specificity reducing the peptide generation, which ultimately lead to the reduction in antidiabetic properties of bioactive peptides. Therefore, the biological activity of peptides generated depends mainly on the substrate, specificity of enzymes used and hydrolysis conditions used [ 14 - 16 ].
The DH usually increases with the increase in incubation time which correlates with the reduction in bioactive properties of peptides. Suppression of these enzymes leads to delay in carbohydrate digestion which, in turn, increases overall digestion time of carbohydrates. Thereby, glucose is less absorbed due to delayed carbohydrates hydrolysis into glucose, and hence, the postprandial blood glucose level and insulin level diminishes [ 19 ].
Our findings revealed that casein hydrolysates generated by different enzymatic treatments show significant antidiabetic properties. The role of such peptides as antidiabetics was revealed and it was observed that chymotrypsin treatment of raw casein yields peptides with maximum antidiabetic activity as compared to those formed by pepsin and trypsin treatment.
It means this property is adversely influenced by boiling. Increase in the temperature denatures milk proteins and reduces the enzymatic specific and activity, leading to significant decrease in the peptide content.
Thus, boiling indirectly and adversely influences the formation of bioactive antidiabetic peptides. It can be concluded that bioactive peptides derived from chymotrypsin and pepsin treatment of raw milk exhibiting maximum antidiabetic activity, could be used as a nutritional supplement for diabetic patients.
Moreover, sheep casein peptides generated by enzymatic treatments exhibiting a significant effect on lowering blood glucose level may be further explored to sequence and identify the individual peptides involved in imparting antidiabetic activity.
Further in-vitro studies are essential to explore the commercial importance of these bioactive peptides as nutritional formulations for diabetic patients. RJ was the co-guide involved in the manuscript preparation.
All authors read and approved the final manuscript. The authors are thankful to the Dolphin PG Institute of Biomedical and Natural Sciences for providing all the necessary chemicals and laboratory facility for this research work. National Center for Biotechnology Information , U. Journal List Vet World v. Vet World. Published online Oct Author information Article notes Copyright and License information Disclaimer. Corresponding author: Santosh Kumar, e-mail: moc. Received May 30; Accepted Sep Open Access.
This article is distributed under the terms of the Creative Commons Attribution 4. This article has been cited by other articles in PMC. Abstract Aim: Sheep milk-born bioactive peptides have been found to exhibit various physiological activities. Materials and Methods: In this investigation, casein prepared from raw and boiled sheep milk was hydrolyzed by three commercially available proteases trypsin, pepsin, and chymotrypsin. Results: Among the three different enzyme hydrolysates, casein treated with chymotrypsin shows the highest antidiabetic activity among other enzymes.
Conclusion: The result obtained hence shows that the effect of boiling on the properties of bioactive peptides released during different enzyme digestion depends largely on the enzymatic formulation used and treatment conditions.
Introduction Milk protein in recent times has been recognized to exhibit numerous functionalities in vivo by the presence of various bioactive peptides [ 1 ]. Hence, these peptides must be incorporated in the form of major ingredients of nutraceutical supplements, dietary formulations, and even in pharmaceutical preparations with the purpose of fulfilling the specific health needs of individuals suffering from specific metabolic disorder In the current study, three different commercially available proteases were employed in the hydrolysis of sodium caseinate obtained from sheep milk.
Materials and Methods Ethical approval Ethical approval is not required to pursue this type of study. Hydrolysis of casein Casein prepared was treated with three different enzymes according to the method of Abubakar et al.
Table-1 Conditions employed for hydrolysis of sheep milk casein. Open in a separate window. Results The dry weight of casein was found to be 3. Table-2 DH of sheep casein by different proteases. Table-3 Antidiabetic status of sheep casein hydrolysates. Discussion Casein prepared isoelectrically was treated with three different enzymes so as to break the caseinates into peptides having desired biological activities.
Conclusion Our findings revealed that casein hydrolysates generated by different enzymatic treatments show significant antidiabetic properties. At temperatures around boiling, the chemical bonds that hold together the structure of enzymes begin to break down. The resulting loss of three-dimensional structure causes enzymes to no longer fit their target substrate molecules, and enzymes entirely stop functioning.
This loss of structure, known as denaturation, is irreversible — once enzymes are heated so much that the chemical bonds holding them together break down, they will not spontaneously form again if temperatures decrease. This is unlike freezing, which does not affect enzyme structure — if temperatures are increased after freezing, enzyme activity will be restored.
Michael Graw has been writing and editing science journalism since Types of Bonding in Crystals. What Is the Role of Enzymes in Metabolism? What Makes an Ice Cube Melt?
How Does Salt Melt Ice? Write down your conclusion from this experiment. This should include answers to questions such as :. What does pepsin do to the protein in egg white?
What other factors are needed? Are they absolutely necessary? Add about 1 ml of copper sulphate solution; the colour should change to a deeper blue. Mix carefully. This is biuret reagent.
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