Collagen Peptides Research Studies
There has been a rise in the number of industries interested in peptides in recent years. Studies suggest that bioactive peptides may be a potential new class of compounds that may bridge the gap between small molecules and protein compounds due to their perceived high potency, specificity, and reportedly favorable profile. Research suggests peptides may have helpful tissue penetration and the capacity to bind with endogenous receptors in a particular and high-affinity manner. Research into peptides as flexible tools for biological discovery and delivery has been motivated by their alleged positive characteristics. Investigations purport that because of their regulatory actions that may lead to physiological impacts, bioactive peptides produced from dietary protein sources have become active components in functional foods and nutraceuticals.
Peptides that may protect collagen against oxidation are a current research topic. However, the age and architecture of collagen-rich tissues, which may dictate a change in tissue structure and composition and, therefore, bioactivity, have received little to no attention in the literature. Furthermore, very little study has been done to evaluate the antioxidant activity of peptides in the dietary matrix. The purpose of this study was to examine the impact of different enzymes and the age and architecture of bovine bones on the antioxidant activity of collagen peptides. Bovine femur and tibia collagen were removed using six enzymes to facilitate peptide release. Researchers examined the effects of heating lipids and proteins from bovine flesh from room temperature to 80 °C on their redox potential, their potential to quench stable free radicals, and their antioxidant activity. There appeared to be a strong interaction between age and anatomy, with the latter having the greatest impact as one age. The effects of the enzymes varied with age and body type. Collagen from juvenile bones hydrolyzed with papain yielded the most peptides. Findings implied that, except for animal proteins, antioxidant activity appeared to increase with increasing temperature. Studies suggest that efficient employment of collagen bioactive peptides may be facilitated by studying the impact of age and the architecture of collagen-rich tissues.
Collagen Peptides Research Studies
Worldwide, researchers have tested collagen peptides isolated from animal tissues for various biological functions. Several industries, including food, nutrition, materials and biomaterials, and sensors, have suggested great promise. Antioxidant, antihypertensive, antidiabetic, anti-inflammatory, immunomodulatory, opioid agonist, wound healing, substance carrier, mineral binding, and support for producing native collagen are some hypothesized actions. Numerous marine and animal tissues have been studied. The potential of some important biological parameters, such as the anatomy of collagen-rich tissues and the age of the animal (or marine) species, on the bioactivity of the collagen peptides, has not been assessed in any of the research reported in the literature, even though many enzymes and hydrolysis parameters have been tested and optimized. Peptides from pig and bovine hemoglobin have been the primary focus of the limited research conducted to evaluate the potential of bioactive peptides on the food matrix.
Therefore, the purpose of this research is to examine the potential of age and bone structure on the bioactivity of collagen peptides liberated by distinct enzymes and from three different classes of proteases in bovine (cow) bones. Given that bone is the most abundant by-product (in terms of volume and weight) of bovines slaughtered for meat consumption and after milk production, it can be considered the most abundant source of collagen, and in particular, type I collagen.
This study aspires to advance the state-of-the-art by providing fresh information on how the age and structure of a bovine’s bones may affect the antioxidant activity of collagen peptides and, more specifically, how this activity translates to the antioxidant power of collagen peptides in a food matrix. Given that oxidative stress has been linked to the development of several disorders, including hypertension, diabetes, obesity, dyslipidemia, cardiovascular difficulties, etc., antioxidant capability was selected from among many different bioactivities. Lipids and proteins from bovine flesh were tested for oxidative stability, redox potential, and antioxidant capability. The thermal stability of collagen peptides was evaluated, as well as the impact of heating from room temperature to 80 °C on the kinetics of redox potential and radical quenching.
Collagen Peptides- Potential Antioxidant Activity
Findings suggested that the antioxidant activity of collagen peptides seemed to vary by enzyme and bone age/structure and was not necessarily proportional to peptide content. The temperature appeared to have a considerable impact on the redox potential, as measured by the ferric to ferrous iron reducing antioxidant power (FRAP) value, with TY peptide solutions being the most useful, excluding the use of expertise.
Scientists interested in further investigations can buy collagen peptides from the Biotech Peptides website. Please note that none of the substances mentioned in this paper have been approved for human consumption, and this article is meant for educational purposes only. Peptides should only be purchased and utilized by licensed professionals, scientists, and academics.
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