260
Antimicrobial activity of bioactive peptides is displayed by various mechanisms
such as prebiotic effect, peptides that are able to block attachment or invasion of
pathogen microorganism, or peptides that could induce a killing or inhibiting effect
on the growth of microorganism (Hernández-Ledesma et al. 2014). Milk-derived
antimicrobial peptides contain highly positive charged sequence. Thus, the net positive charge may help in binding of the peptides to negatively charged bacterial
membranes. Also, the amphiphilic nature of peptides aids in bacterial membrane
disruption (Hernández-Ledesma et al. 2014). Milk derived antimicrobial activity is
attributed to factors like immunoglobulins, lysozyme, lactoferrin and lactoperoxidase inherently present in milk proteins (Jabbari et al. 2012). Thus, dairy proteins
act as precursors for antimicrobial peptides which can boost an organism’s natural
defense system against pathogens (Pellegrini 2003).
The fragment 17–41 of lactoferrin (also known as lactoferricin) has shown
potent antimicrobial activity due to its attachment to the lipid A part of bacterial
lipopolysaccharides, along with increased membrane permeability (Cicero et al.
2017). Enzymatic hydrolysates of lactoferrin has displayed more antimicrobial
activity than that of parent protein (Tomita et al. 1991). also, peptides purified from
bovine lactoferrin has shown high antibacterial activity against Gram-positive and
Gram- negative bacteria (Wakabayashi et al. 2003). Whey proteins like
β-lactoglobulin and α-lactalbumin are said to have broad spectrum antimicrobial
potential (Sultan et al. 2017). Tryptic hydrolysate of whey protein generated two
anionic peptides that exhibited growth inhibition activity against Listeria monocytogenes and Staphylococcus aureus (Demers Mathieu et al. 2013). Casein proteins
too are a good source of antimicrobial peptides (Expósito and Recio 2006). Thus,
peptides from milk proteins could be used as potential antimicrobial agents in food
industries.
Conclusions
There are peptide fragments encrypted within the structure of food proteins that
show biological functions upon release. The bioactivities of the peptides are wide
ranging; antioxidative, antimicrobial, antihypertensive, anticancer, anti-diabetic,
opioid, mineral binding and anti-inflammatory. Thus, bioactive peptides could
potentially be used to reduce risk and prevent chronic diseases like diabetes mellitus, hypertension, obesity and cancer. It is speculated that with more in vivo studies
designed around long-term randomized-control clinical trials will further elucidate
the mechanism by which bioactive peptides showcase their physiological effects.
Their potential application in the food industry is an exciting and novel prospect
which will contribute to improving human health.
S. Maqsood et al.
Antimicrobial activity of bioactive peptides is displayed by various mechanisms
such as prebiotic effect, peptides that are able to block attachment or invasion of
pathogen microorganism, or peptides that could induce a killing or inhibiting effect
on the growth of microorganism (Hernández-Ledesma et al. 2014). Milk-derived
antimicrobial peptides contain highly positive charged sequence. Thus, the net positive charge may help in binding of the peptides to negatively charged bacterial
membranes. Also, the amphiphilic nature of peptides aids in bacterial membrane
disruption (Hernández-Ledesma et al. 2014). Milk derived antimicrobial activity is
attributed to factors like immunoglobulins, lysozyme, lactoferrin and lactoperoxidase inherently present in milk proteins (Jabbari et al. 2012). Thus, dairy proteins
act as precursors for antimicrobial peptides which can boost an organism’s natural
defense system against pathogens (Pellegrini 2003).
The fragment 17–41 of lactoferrin (also known as lactoferricin) has shown
potent antimicrobial activity due to its attachment to the lipid A part of bacterial
lipopolysaccharides, along with increased membrane permeability (Cicero et al.
2017). Enzymatic hydrolysates of lactoferrin has displayed more antimicrobial
activity than that of parent protein (Tomita et al. 1991). also, peptides purified from
bovine lactoferrin has shown high antibacterial activity against Gram-positive and
Gram- negative bacteria (Wakabayashi et al. 2003). Whey proteins like
β-lactoglobulin and α-lactalbumin are said to have broad spectrum antimicrobial
potential (Sultan et al. 2017). Tryptic hydrolysate of whey protein generated two
anionic peptides that exhibited growth inhibition activity against Listeria monocytogenes and Staphylococcus aureus (Demers Mathieu et al. 2013). Casein proteins
too are a good source of antimicrobial peptides (Expósito and Recio 2006). Thus,
peptides from milk proteins could be used as potential antimicrobial agents in food
industries.
Conclusions
There are peptide fragments encrypted within the structure of food proteins that
show biological functions upon release. The bioactivities of the peptides are wide
ranging; antioxidative, antimicrobial, antihypertensive, anticancer, anti-diabetic,
opioid, mineral binding and anti-inflammatory. Thus, bioactive peptides could
potentially be used to reduce risk and prevent chronic diseases like diabetes mellitus, hypertension, obesity and cancer. It is speculated that with more in vivo studies
designed around long-term randomized-control clinical trials will further elucidate
the mechanism by which bioactive peptides showcase their physiological effects.
Their potential application in the food industry is an exciting and novel prospect
which will contribute to improving human health.
S. Maqsood et al.