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  1. Fulltext Response Factorial Design Analysis on Papain-Generated Hydrolysates from Actinopyga lecanora for Determination of Antioxidant and Antityrosinase Activities
    Bahari AN, Saari N, Salim N, Ashari SE
    Molecules, 2020 Jun 08;25(11).
    PMID: 32521731 DOI: 10.3390/molecules25112663
    Actinopyga lecanora (A. lecanora) is classified among the edible species of sea cucumber, known to be rich in protein. Its hydrolysates were reported to contain relatively high antioxidant activity. Antioxidants are one of the essential properties in cosmeceutical products especially to alleviate skin aging. In the present study, pH, reaction temperature, reaction time and enzyme/substrate ratio (E/S) have been identified as the parameters in the papain enzymatic hydrolysis of A. lecanora. The degree of hydrolysis (DH) with antioxidant activities of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric-reducing antioxidant power (FRAP) assays were used as the responses in the optimization. Analysis of variance (ANOVA), normal plot of residuals and 3D contour plots were evaluated to study the effects and interactions between parameters. The best conditions selected from the optimization were at pH 5.00, 70 °C of reaction temperature, 9 h of hydrolysis time and 1.00% enzyme/substrate (E/S) ratio, with the hydrolysates having 51.90% of DH, 42.70% of DPPH activity and 109.90 Fe2+μg/mL of FRAP activity. The A. lecanora hydrolysates (ALH) showed a high amount of hydrophobic amino acids (286.40 mg/g sample) that might be responsible for antioxidant and antityrosinase activities. Scanning electron microscopy (SEM) image of ALH shows smooth structures with pores. Antityrosinase activity of ALH exhibited inhibition of 31.50% for L-tyrosine substrate and 25.40% for L-DOPA substrate. This condition suggests that the optimized ALH acquired has the potential to be used as a bioactive ingredient for cosmeceutical applications.
    Matched MeSH terms: Protein Hydrolysates/pharmacology*
  2. Partially hydrolyzed formula in non-exclusively breastfed infants: A systematic review and expert consensus
    Vandenplas Y, Latiff AHA, Fleischer DM, Gutiérrez-Castrellón P, Miqdady MS, Smith PK, et al.
    Nutrition, 2019 01;57:268-274.
    PMID: 30223233 DOI: 10.1016/j.nut.2018.05.018
    OBJECTIVES: Guidance and evidence supporting routine use of partially hydrolyzed formula (pHF) versus intact cows' milk protein (CMP) formula are limited in non-exclusively breastfed infants. The aim of this review was to better clarify issues of routine use of pHF in non-exclusively breastfed infants who are not at risk for allergic disease by using a systematic review and Delphi Panel consensus.

    METHODS: A systematic review and Delphi consensus panel (consisting of eight8 international pediatric allergists and gastroenterologists) was conducted to evaluate evidence supporting growth, tolerability, and effectiveness of pHF in non-exclusively breastfed infants.

    RESULTS: None of the studies reviewed identified potential harm of pHF use compared with CMP in non-exclusively breastfed infants. There was an expert consensus that pHF use is likely as safe as intact CMP formula, given studies suggesting these have comparable nutritional parameters. No high-quality studies were identified evaluating the use of pHF to prevent allergic disease in non-exclusively breastfed infants who are not at risk for allergic disease (e.g., lacking a parental history of allergy). Limited data suggest that pHF use in non-exclusively breastfed infants may be associated with improved gastric emptying, decreased colic incidence, and other common functional gastrointestinal symptoms compared with CMP. However, because the data are of insufficient quality, the findings from these studies have to be taken with caution. No studies were identified that directly compared the different types of pHF, but there was an expert consensus that growth, allergenicity, tolerability, effectiveness, and clinical role among such pHF products may differ.

    CONCLUSIONS: Limited data exist evaluating routine use of pHFs in non-exclusively breastfed infants, with no contraindications identified in the systematic review. An expert consensus considers pHFs for which data were available to be as safe as CMP formula as growth is normal. The preventive effect on allergy of pHF in infants who are not at risk for allergic disease has been poorly studied. Cost of pHF versus starter formula with intact protein differs from country to country. However, further studies in larger populations are needed to clinically confirm the benefits of routine use of pHF in non-exclusively breastfed infants. These studies should also address potential consumer preference bias.

    Matched MeSH terms: Protein Hydrolysates/pharmacology*
  3. Identification of two novel antioxidant peptides from edible bird's nest (Aerodramus fuciphagus) protein hydrolysates
    Ghassem M, Arihara K, Mohammadi S, Sani NA, Babji AS
    Food Funct, 2017 May 24;8(5):2046-2052.
    PMID: 28497137 DOI: 10.1039/c6fo01615d
    Edible bird's nest (EBN) is widely consumed as a delicacy and traditional medicine amongst the Chinese. In the present study, for the first time, the antioxidant properties of an EBN pepsin-trypsin hydrolysate of the swiftlet species Aerodramus fuciphagus and its ultrafiltration fractions were investigated. Thirteen peptides with molecular weights between 514.29 and 954.52 Da were identified in the EBN fraction with the use of mass spectrometry. Two novel pentapeptides Pro-Phe-His-Pro-Tyr and Leu-Leu-Gly-Asp-Pro, corresponding to f134-138 and f164-168 of cytochrome b of A. fuciphagus, indicated the highest ORAC values of 14.95 and 14.32 μM of TE μM(-1) peptide, respectively. Both purified peptides showed resistance against simulated gastrointestinal proteases. In addition, both peptides had no in vitro cytotoxicity on human lung MRC-5 cells and prevented human liver carcinoma HepG2 cellular damage caused by hydroxyl radicals. Therefore, it is suggested that EBN protein hydrolysates are a good source of natural antioxidants and could be applied as nutraceutical compounds.
    Matched MeSH terms: Protein Hydrolysates/pharmacology
  4. Fulltext Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments
    Laosam P, Panpipat W, Yusakul G, Cheong LZ, Chaijan M
    PLoS One, 2021;16(10):e0258445.
    PMID: 34695136 DOI: 10.1371/journal.pone.0258445
    The production of bioactive peptides from animal-based raw materials highly depends on enzymatic hydrolysis. Porcine placenta is an underutilized biomass in Thailand's pig farms, yet it is still a source of proteins and beneficial compounds. Porcine placenta could be used as a protein substrate for the production of enzymatic hydrolysate, which could be employed as a functional food ingredient in the future. The goal of this study was to enzymatically produce porcine placenta hydrolysates (PPH) using three commercial enzymes (Alcalase, Flavouzyme, and papain) and evaluate their in vitro antioxidant and antibacterial activity. The degree of hydrolysis (DH) increased as the enzyme load and hydrolysis time increased, but the DH was governed by the enzyme class. The maximum DH was found after using 10% enzyme for 20 min of hydrolysis (36.60%, 31.40%, and 29.81% for Alcalase, Flavouzyme, and papain). Depending on the enzyme type and DH, peptides of various sizes (0.40-323.56 kDa) were detected in all PPH. PPH created with Alcalase had an excellent reducing capacity and metal chelating ability (p < 0.05), whereas PPH made with Flavourzyme and Papain had higher DPPH• and ABTS•+ inhibitory activities (p < 0.05). Papain-derived PPH also had a strong antibacterial effect against Staphylococcus aureus and Escherichia coli, with clear zone values of 17.20 mm and 14.00 mm, respectively (p < 0.05). When PPH was transported via a gastrointestinal tract model system, its antioxidative characteristics were altered. PPH's properties and bioactivities were thus influenced by the enzyme type, enzyme concentration, and hydrolysis time used. Therefore, PPH produced from porcine placenta can be categorized as an antioxidant and antibacterial alternative.
    Matched MeSH terms: Protein Hydrolysates/pharmacology
  5. Purification and characterisation of antibacterial peptide-containing compound derived from palm kernel cake
    Tan YN, Ayob MK, Wan Yaacob WA
    Food Chem, 2013 Jan 1;136(1):279-84.
    PMID: 23017424 DOI: 10.1016/j.foodchem.2012.08.012
    Palm kernel cake (PKC), the most useful by-product resulted from palm kernel oil production. In this study, PKC-derived protein product was found suitable for use as an antimicrobial agent with potent antibacterial activity, particularly against Bacillus species, after enzymatic hydrolysis with alcalase. The hydrolysate was further purified by gel filtration chromatography. The purified fraction was found to have 14.63±0.70% (w/w) protein, a molecular mass of 2.4kDa and low hemolytic activity (<50% hemolysis of human erythrocytes at concentration of 1000μg/ml). The presence of lysine and the major component lauric acid derivative, as indicated by electrospray ionisation-mass spectrometry (ESI-MS) direct infusion and nuclear magnetic resonance (NMR) spectroscopy, may have contributed to the antibacterial effect of purified PKC fraction. This study suggests that the antibacterial PKC compound may be not a pure peptide but instead a peptide-containing compound high in lauric acid derivative.
    Matched MeSH terms: Protein Hydrolysates/pharmacology
  6. Angiotensin-I Converting Enzyme (ACE) Inhibitory and Anti-Hypertensive Effect of Protein Hydrolysate from Actinopyga lecanora (Sea Cucumber) in Rats
    Sadegh Vishkaei M, Ebrahimpour A, Abdul-Hamid A, Ismail A, Saari N
    Mar Drugs, 2016 Sep 30;14(10).
    PMID: 27706040
    Food protein hydrolysates are known to exhibit angiotensin converting enzyme (ACE) inhibitory properties and can be used as a novel functional food for prevention of hypertension. This study evaluated the ACE inhibitory potentials of Actinopyga lecanora proteolysate (ALP) in vivo. The pre-fed rats with ALP at various doses (200, 400, 800 mg/kg body weight) exhibited a significant (p ≤ 0.05) suppression effect after inducing hypertension. To determine the optimum effective dose that will produce maximal reduction in blood pressure, ALP at three doses was fed to the rats after inducing hypertension. The results showed that the 800 mg/kg body weight dose significantly reduced blood pressure without noticeable negative physiological effect. In addition, there were no observable changes in the rats' heart rate after oral administration of the ALP. It was concluded that Actinopyga lecanora proteolysate could potentially be used for the development of functional foods and nutraceuticals for prevention and treatment of hypertension.
    Matched MeSH terms: Protein Hydrolysates/pharmacology*
  7. Fulltext Identification, structure-activity relationship and in silico molecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish (Actinopyga lecanora) hydrolysates
    Auwal SM, Zainal Abidin N, Zarei M, Tan CP, Saari N
    PLoS One, 2019;14(5):e0197644.
    PMID: 31145747 DOI: 10.1371/journal.pone.0197644
    Stone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including Ala-Leu-Gly-Pro-Gln-Phe-Tyr (794.44 Da), Lys-Val-Pro-Pro-Lys-Ala (638.88 Da), Leu-Ala-Pro-Pro-Thr-Met (628.85 Da), Glu-Val-Leu-Ile-Gln (600.77 Da) and Glu-His-Pro-Val-Leu (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.310 mM, 1.440 mM and 1.680 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.
    Matched MeSH terms: Protein Hydrolysates/pharmacology*
  8. Generation, Fractionation, and Characterization of Iron-Chelating Protein Hydrolysate from Palm Kernel Cake Proteins
    Zarei M, Ghanbari R, Tajabadi N, Abdul-Hamid A, Bakar FA, Saari N
    J Food Sci, 2016 Feb;81(2):C341-7.
    PMID: 26720491 DOI: 10.1111/1750-3841.13200
    Palm kernel cake protein was hydrolyzed with different proteases namely papain, bromelain, subtilisin, flavourzyme, trypsin, chymotrypsin, and pepsin to generate different protein hydrolysates. Peptide content and iron-chelating activity of each hydrolysate were evaluated using O-phthaldialdehyde-based spectrophotometric method and ferrozine-based colorimetric assay, respectively. The results revealed a positive correlation between peptide contents and iron-chelating activities of the protein hydrolysates. Protein hydrolysate generated by papain exhibited the highest peptide content of 10.5 mM and highest iron-chelating activity of 64.8% compared with the other hydrolysates. Profiling of the papain-generated hydrolysate by reverse phase high performance liquid chromatography fractionation indicated a direct association between peptide content and iron-chelating activity in most of the fractions. Further fractionation using isoelectric focusing also revealed that protein hydrolysate with basic and neutral isoelectric point (pI) had the highest iron-chelating activity, although a few fractions in the acidic range also exhibited good metal chelating potential. After identification and synthesis of papain-generated peptides, GGIF and YLLLK showed among the highest iron-chelating activities of 56% and 53%, whereas their IC50 were 1.4 and 0.2 μM, respectively.
    Matched MeSH terms: Protein Hydrolysates/pharmacology*
  9. Fulltext Actinopyga lecanora hydrolysates as natural antibacterial agents
    Ghanbari R, Ebrahimpour A, Abdul-Hamid A, Ismail A, Saari N
    Int J Mol Sci, 2012;13(12):16796-811.
    PMID: 23222684 DOI: 10.3390/ijms131216796
    Actinopyga lecanora, a type of sea cucumber commonly known as stone fish with relatively high protein content, was explored as raw material for bioactive peptides production. Six proteolytic enzymes, namely alcalase, papain, pepsin, trypsin, bromelain and flavourzyme were used to hydrolyze A. lecanora at different times and their respective degrees of hydrolysis (DH) were calculated. Subsequently, antibacterial activity of the A. lecanora hydrolysates, against some common pathogenic Gram positive bacteria (Bacillus subtilis and Staphylococcus aureus) and Gram negative bacteria (Escherichia coli, Pseudomonas aeruginosa, and Pseudomonas sp.) were evaluated. Papain hydrolysis showed the highest DH value (89.44%), followed by alcalase hydrolysis (83.35%). Bromelain hydrolysate after one and seven hours of hydrolysis exhibited the highest antibacterial activities against Pseudomonas sp., P. aeruginosa and E. coli at 51.85%, 30.07% and 30.45%, respectively compared to the other hydrolysates. Protein hydrolysate generated by papain after 8 h hydrolysis showed maximum antibacterial activity against S. aureus at 20.19%. The potent hydrolysates were further fractionated using RP-HPLC and antibacterial activity of the collected fractions from each hydrolysate were evaluated, wherein among them only three fractions from the bromelain hydrolysates exhibited inhibitory activities against Pseudomonas sp., P. aeruginosa and E. coli at 24%, 25.5% and 27.1%, respectively and one fraction of papain hydrolysate showed antibacterial activity of 33.1% against S. aureus. The evaluation of the relationship between DH and antibacterial activities of papain and bromelain hydrolysates revealed a meaningful correlation of four and six order functions.
    Matched MeSH terms: Protein Hydrolysates/pharmacology*
  10. High angiotensin-I converting enzyme (ACE) inhibitory activity of Alcalase-digested green soybean (Glycine max) hydrolysates
    Hanafi MA, Hashim SN, Chay SY, Ebrahimpour A, Zarei M, Muhammad K, et al.
    Food Res Int, 2018 04;106:589-597.
    PMID: 29579964 DOI: 10.1016/j.foodres.2018.01.030
    As a protein-rich, underutilized crop, green soybean could be exploited to produce hydrolysates containing angiotensin-I converting enzyme (ACE) inhibitory peptides. Defatted green soybean was hydrolyzed using four different food-grade proteases (Alcalase, Papain, Flavourzyme and Bromelain) and their ACE inhibitory activities were evaluated. The Alcalase-generated green soybean hydrolysate showed the highest ACE inhibitory activity (IC50: 0.14 mg/mL at 6 h hydrolysis time) followed by Papain (IC50: 0.20 mg/mL at 5 h hydrolysis time), Bromelain (IC50: 0.36 mg/mL at 6 h hydrolysis time) and Flavourzyme (IC50: 1.14 mg/mL at 6 h hydrolysis time) hydrolysates. The Alcalase-generated hydrolysate was profiled based on its hydrophobicity and isoelectric point using reversed phase high performance liquid chromatography (RP-HPLC) and isoelectric point focusing (IEF) fractionators. The Alcalase-generated green soybean hydrolysate comprising of peptides EAQRLLF, PSLRSYLAE, PDRSIHGRQLAE, FITAFR and RGQVLS, revealed the highest ACE inhibitory activity of 94.19%, 99.31%, 92.92%, 101.51% and 90.40%, respectively, while their IC50 values were 878 μM, 532 μM, 1552 μM, 1342 μM and 993 μM, respectively. It can be concluded that Alcalase-digested green soybean hydrolysates could be exploited as a source of peptides to be incorporated into functional foods with antihypertensive activity.
    Matched MeSH terms: Protein Hydrolysates/pharmacology*
  11. Toxicity study and blood pressure-lowering efficacy of whey protein concentrate hydrolysate in rat models, plus peptide characterization
    Hussein FA, Chay SY, Ghanisma SBM, Zarei M, Auwal SM, Hamid AA, et al.
    J Dairy Sci, 2020 Mar;103(3):2053-2064.
    PMID: 31882211 DOI: 10.3168/jds.2019-17462
    We evaluated the acute (single-dose) and subacute (repeated-dose) oral toxicity of alcalase-hydrolyzed whey protein concentrate. Our acute study revealed no death or treatment-related complications, and the median lethal dose of whey protein concentrate hydrolysate was >2,500 mg/kg. In the subacute study, when the hydrolysate was fed at 3 different concentrations (200, 400, and 800 mg/kg), no groups showed toxicity changes compared with controls. Then, whey protein concentrate hydrolysate was orally administered to spontaneously hypertensive rats. Results revealed significant reductions in blood pressure in a dose-dependent manner, and dosing at 400 mg/kg led to significant blood pressure reduction (-47.8 mm Hg) compared with controls (blood pressure maintained) and the findings of previous work (-21 mm Hg). Eight peptides-RHPEYAVSVLLR, GGAPPAGRL, GPPLPRL, ELKPTPEGDL, VLSELPEP, DAQSAPLRVY, RDMPIQAF, and LEQVLPRD-were sequentially identified and characterized. Of the peptides, VLSELPEP and LEQVLPRD showed the most prominent in vitro angiotensin-I converting enzyme inhibition with half-maximal inhibitory concentrations of 0.049 and 0.043 mM, respectively. These findings establish strong evidence for the in vitro and in vivo potential of whey protein concentrate hydrolysate to act as a safe, natural functional food ingredient that exerts antihypertensive activity.
    Matched MeSH terms: Protein Hydrolysates/pharmacology
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