Encapsulation of bioactive whey peptides in soy lecithin-derived nanoliposomes: Influence of peptide molecular weight

Mohan, Aishwarya; McClements, David Julian; Udenigwe, Chibuike C.

doi:10.1016/j.foodchem.2016.06.075

Cited by 100 publications

(58 citation statements)

References 26 publications

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“…Since ACE-inhibitory peptides are generally short chained, enzymes should have a high hydrolysis degree [54,55]. Optimum temperature and pH can be different depending on the enzyme, for example, 50 °C and pH 9.0 for alcalase [56], 50 °C and pH 6.0 for flavourzyme [57], 50 °C and pH 8.0 for thermolysin [35], and 65 °C and pH 7.0 for papain [58]. Alcalase and thermolysin are capable of producing relatively higher ACE-inhibitory active peptides than other proteolytic enzymes [14,26,35,36,40,51,57].…”

Section: Production Of Ace-inhibitory Peptides From Plantsmentioning

confidence: 99%

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

et al. 2017

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Hypertension is an important factor in cardiovascular diseases. Angiotensin-I-converting enzyme (ACE) inhibitors like synthetic drugs are widely used to control hypertension. ACE-inhibitory peptides from food origins could be a good alternative to synthetic drugs. A number of plant-based peptides have been investigated for their potential ACE inhibitor activities by using in vitro and in vivo assays. These plant-based peptides can be obtained by solvent extraction, enzymatic hydrolysis with or without novel food processing methods, and fermentation. ACE-inhibitory activities of peptides can be affected by their structural characteristics such as chain length, composition and sequence. ACE-inhibitory peptides should have gastrointestinal stability and reach the cardiovascular system to show their bioactivity. This paper reviews the current literature on plant-derived ACE-inhibitory peptides including their sources, production and structure, as well as their activity by in vitro and in vivo studies and their bioavailability.

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Section: Production Of Ace-inhibitory Peptides From Plantsmentioning

confidence: 99%

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

et al. 2017

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“…Bioactivity of protein hydrolysates could be affected by the molecular weights of the peptides (Mohan et al, 2016). Table 3 outlines the ABTS radical scavenging activity and the IC 50 value of EBH of the three fractions with different molecular weights.…”

Section: Ultrafiltrationmentioning

confidence: 99%

Isolation, Purification and Characterization of Antioxidative Bioactive Elastin Peptides from Poultry Skin

Nadalian

Kamaruzaman

Yusop

et al. 2019

Food Sci Anim Resour

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Muscle-based by-products are often undervalued although commonly reported having a high amount of natural bioactive peptides. In this study, elastin was isolated from the protein of broiler hen skin while its hydrolysate was prepared using Elastase. Assessment of antioxidative properties of elastin-based hydrolysate (EBH) was based on three different assays; 2,2-diphenyl-1-picryl-hydrazyl-hydrate (DPPH) radical, 2,2'-azinobis (3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) radical and metal chelating ability. The EBH was purified further using ultrafiltration, gel filtration and Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC). The IC50 of ABTS radical activities for EBH were decreased as EBH further purified using ultrafiltration (EBH III; 0.66 mg/mL)>gel filtration (EB-II; 0.42 mg/mL)>RP-HPLC (EB-II4; 0.12 mg/mL). The sequential identification of the peptide was done by matrix-assisted laser desorption/ ionization time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/ TOF-MS) of the potent fractions obtained from RP-HPLC (EB-II4). The presence of hydrophobic amino acids (Val and Pro) in the peptide sequences could potentially contribute to the high antioxidant activity of EBH. The sequences GAHTGPRKPFKPR, GMPGFDVR and ADASVLPK were identified as antioxidant peptides. In conclusion, the antioxidative potential from poultry skin specifically from elastin is evident and can be explored to be used in many applications such as health and pharmaceutical purposes.

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“…However, it should be considered that the difference in zeta potential values are strongly associated with the type, composition, and purity of the material used to form liposomes. In this regard, based on the findings of Mohan, McClements, and Udenigwe (), whey peptide‐loaded liposomes formed using the only lecithin had zeta potential values ranging between −63.9 and −72.4 mV, while empty liposomes had −55 mV.…”

Section: Resultsmentioning

confidence: 96%

“…of Mohan, McClements, and Udenigwe (2016), whey peptide-loaded liposomes formed using the only lecithin had zeta potential values ranging between −63.9 and −72.4 mV, while empty liposomes had −55 mV.…”

mentioning

confidence: 97%

Antimicrobial and antioxidant properties of burgers with quinoa peptide‐loaded nanoliposomes

Yekta

Rezaei

Nouri

et al. 2019

Journal of Food Safety

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This study was aimed to examine the antioxidant (thiobarbituric acid reactive substances [TBARS], peroxide value [PV], and as well as antimicrobial (total bacterial count, Staphylococcus aureus [S. aureus], mold and yeast counts) activities and spoilage indices (total volatile base nitrogen [TVB‐N]) of quinoa peptide‐loaded liposomes incorporated into burger during 12 days of refrigerated storage. Among four prepared batches, the lowest TBARS, PV, and TVB‐N values (0.281 ± 0.05 mg MDA/kg, 3.25 ± 0.34 mEq/kg and 18.65 ± 0.88%, respectively) were correlated with T3 treatment (5 mg/ml peptide). A significant different in the antimicrobial activity among each treatment after 12 days of storage was noted. At the end of refrigerated storage, the highest mean of total bacterial count, S. aureus, mold and yeast (8.36 ± 0.22, 4.19 ± 0.2, and 3.28 ± 0.05 log CFU/g, respectively) were observed in control group, while the lowest corresponded values (3.95 ± 0.2, 2.52 ± 0.25, and 1.52 ± 0.02 log CFU/g, respectively) were noted in T3 treatment. The results showed that the antimicrobial and antioxidant properties of the examined burgers were improved by incorporation of liposomes quinoa peptides encapsulated.

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Encapsulation of bioactive whey peptides in soy lecithin-derived nanoliposomes: Influence of peptide molecular weight

Cited by 100 publications

References 26 publications

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants

Isolation, Purification and Characterization of Antioxidative Bioactive Elastin Peptides from Poultry Skin

Antimicrobial and antioxidant properties of burgers with quinoa peptide‐loaded nanoliposomes

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