Proteins (tissues) | Bioactive peptides (functionalities) | Processing conditions for preparing hydrolysates or peptidesa | Product characterization | References |
---|---|---|---|---|
Raw meat | Antioxidant peptides | - Prepared by flavourzyme or alcalase simultaneously or sequentially (E/S 1–3%, 50–55 °C, pH 6.5–7.5 for up to 6 h) | - The hydrolysate after a sequential hydrolysis using alcalase and flavourzyme showed higher degree of hydrolysis - Flavourzyme-digested hydrolysate showed higher protein recovery and antioxidant activity (DPPH-scavenging activity, FRAP, and FICA) | Kumar et al. (2020) |
Raw meat | Antioxidant activity, bioaccessibility, and solubility | - Prepared by Flavourzyme (E/S 3%, pH 6.6, 54 °C, 30 min) - Dried either spray-drying (SD) or freeze-drying (FD) | - FRAP: SD > FD - DPPH-scavenging activity: SD > FD - Particle size: SD < FD - Flowability: SD > FD - Bioaccessibility: SD > FD - Protein content SD < FD - Solubility: SD < FD | Kumar et al. (2021) |
Raw meat | Antioxidant and ACEi activities | - Prepared by alcalase (55 °C, pH 7.0), flavourzyme (50 °C, pH 7.0), neutrase (50 °C, pH 6.0), protamex (40 °C, pH 7.0), pepsin (37 °C, pH 3.0) and trypsin (37 °C, pH 8.0) for up to 6 h (E/S 1%) - Added hydrolysates into crab meat analogue | - Incorporation of 1.5% of the hydrolysate increased DPPH- and hydroxyl radical-scavenging activities of crab meat analogue - Incorporation of 1.0% of the hydrolysate increased ACEi activity of crab meat analogue | Jin et al. (2016) |
Raw meat | Antioxidant activity | - Prepared by Protamex (E/S 5%, 43 °C, pH 7.0) for 1 h followed by Bromelain (E/S 1%, 50 °C, pH 7.0) - Added 1% or 4% hydrolysate powder (dry basis) into boiled fish paste followed by storage at 10 °C over 4 weeks | - Antioxidant activity (DPPH-scavenging activity) of boiled fish paste was increased - Physicochemical and sensory properties were reduced | Hur et al. (2016) |
Muscle proteins | Renin, ACEi, antioxidant, and antihypertensive activities | - Prepared by pepsin (E/S 1%, pH 2.0) at 37 °C for 1.5 h - Prepared by pepsin (E/S 1%, pH 2.0, 1.5 h) and pancreatin (E/S 1%, pH 7.5, 3 h) at 37 °C sequentially | - Renin inhibition (IC50 value: 0.34–0.52 mg/mL) - ACE inhibition (IC50 value: 0.42–0.65 mg/mL) - Bovine plasma oxidation-inhibitory activity (plasma sulfhydryl content and FRAP) - Reduced systolic blood pressure by 26.5 and 36.8 mmHg in spontaneously hypertensive rats | Udenigwe et al. (2017) |
Muscle proteins | Antioxidant, ACEi, and anti-inflammatory peptides (IWHHT, IWH, IW) | - IWHHT was prepared by thermolysin (E/S 0.5%, 60 °C, pH 8 for 3 h) - IWH and IW were gastrointestinal digests of IWHHT | - IWHHT/IW had ACE IC50 values of 9.93/2.0 µM - IWHHT, IWH, and IW reduced basal oxidative stress in endothelial cells (DHE staining assay) - IWHHT and IWH attenuated TNFα-induced inflammation (reduced VCAM-1 expression by 40–60%) in endothelial cells - IWHHT, IWH, and IW were transported intact in Caco-2 cell monolayers | |
Muscle proteins | Anti-inflammatory peptides (WPW, FLWGKSY, AGLLGLL, SFMNVKHWPW, AFMNVKHWPW, TFLPMLQHIS, ASLSTFQQMWITK | - Prepared by Protex 50FP (E/S 4%, 50 °C, pH 3.0 for 3 h) | - The hydrolysate increased interleukin-10 level in Sprague-Dawley rats - The hydrolysate and derived peptides showed in vitro interleukin-6 inhibitory activity in endotoxin-activated macrophage-like U937 cells | |
Muscle proteins | Antioxidant, anti-inflammatory, ACEi, and ACE2u activities | - Prepared by 9 enzymes (E/S 4%, 3 h) individually or in combination, including alcalase (pH 8, 50 °C), Protex 6L (pH 8, 37 °C), Protease S (pH 8, 37 °C), thermoase (pH 8, 60 °C), trypsin (pH 8, 60 °C), protease M (pH 8, 60 °C), pepsin (pH 2, 60 °C), Protex 50FP (pH 3, 60 °C), and Protex 26L (pH 3, 60 °C) | - 18 hydrolysates were prepared; 3 hydrolysates prepared by Protex 26L, pepsin, or thermoase showed high multifunctional bioactivities and peptide yield - Thermoase-digested hydrolysate maintained its bioactivities after gastrointestinal digestion and transport across Caco-2 cells - Thermoase-digested hydrolysate reduced blood pressure in spontaneously hypertensive rats in a preliminary trial | Fan et al. (2020) |
Muscle proteins | Blood pressure reduction | - Prepared by thermoase (pH 8, 60 °C, 3 h) - The hydrolysate was orally administrated at 1 g/kg body weight to spontaneously hypertensive rats, with blood pressure monitor 24 h per day every 2 days rover 20 days | - Thermoase-digested hydrolysate reduced systolic blood pressure from 168.7 to 156.8 mmHg - Modulated the renin–angiotensin system components (increased plasma and vascular levels of ACE2 and angiotensin (1-7); reduced plasma angiotensin II concentrations - Attenuated vascular inflammation, oxidative stress and fibrosis | |
Muscle proteins | ACEi, ACE2u, and antioxidant peptides | - Prepared by thermoase (E/S 4%, pH 8, 60 °C, 3 h) | - 5 ACEi peptides (IC50 values of 0.034–5.77 μg/mL): VRP, LKY, VRY, KYKA, and LKYKA - 4 ACE2u peptides (increased vascular ACE2 expression by 0.52–0.84 folds): VKW, VHPKESF, VVHPKESF and VAQWRTKYETDAIQRTEELEEAKKK - 4 peptides (VRP, LKY, VRY, and VVHPKESF) showed antioxidant activity in vascular cells | |
Muscle proteins | Human bitter taste receptor-blockers | - Prepared by Protease S, alcalase, Protex 6L, and Protex 50FP were assessed on their bitter taste receptor-blockers by electronic tongue and also in HEK293T cells | - The Protex 50FP-digested hydrolysate has the lowest bitterness - A number of peptides identified from Protex 50FP-digested hydrolysate inhibited quinine- and diphenhydramine-mediated bitter sensation | Xu et al. (2019) |
Elastin (Skin) | Antioxidant peptides | - Prepared by alcalase (pH 8.5, 60 °C) and elastase (pH 8.5, 37 °C) for 2, 4, 8, 12, 16 or 24 h | - DPPH-scavenging activity (16–50%) - ABTS-scavenging activity (60–79%) - Fe2+ chelating activities (50–77%) | Nadalian et al. (2015) |
Elastin (Skin) | ACEi activity | - Prepared by alcalase (pH 8.5, 60 °C) and elastase (pH 8.5, 37 °C) for 2, 4, 8, 12, 16 or 24 h | - Both elastin hydrolysates and its fraction (< 3 kDa) exhibited ACEi activity | Yusop et al. (2016) |
Collagen (from meat) | Antioxidant, anti-inflammatory, proliferative, and type I collagen synthetic activities | - Prepared by protease M (pH 3.0), alcalase (pH 8.0), Protex 50FP (pH 3.0), Protex 51FP (pH 7.5), by an individual enzyme (2 h) or in combination (2 h for each enzyme) (E/S 2%, 50 °C) (10 hydrolysates) | In TNFα-stimulated human dermal fibroblasts - Five hydrolysates reduced oxidative stress - Six hydrolysates reduced inflammation (inhibited ICAM-1 and VCAM-1 expressions) - Two hydrolysates promoted cellular proliferation - One hydrolysate increased type I procollagen synthesis | Offengenden et al. (2018) |
Collagen (Skin) | LWM peptides | - Pepsin (E/S 1%, pH 2.0) for 24 h of pretreatment followed by hydrolysis by papain (E/S 2%, pH 6.0, 60 °C, 6 h) | - Pepsin treatment enhanced production of LMW collagen peptides (to 32.59%) by removing telopeptides and reduces cross-links | Hong et al. (2017) |
Collagen (Skin) | LMW peptides | - Formic acid treatment of pepsin- (E/S 1%, pH 2.0, 24 h) or heat-soluble collagens, before hydrolysis by papain (E/S 2%, pH 6.0, 60 °C, 6 h) | - Formic acid treatment enhanced production of LMW collagen peptides (from 36.32 to 43.34%) for pepsin-soluble or (33.79–48.92%) for heat-soluble collagen by removing telopeptides and reducing cross-links | Hong et al. (2018) |
Collagen (Skin) | LMW peptides | - α-amylase pretreatment (E/S 2%, pH 5.4, 20 °C, 6 h) followed by hydrolysis by papain (E/S 5%, pH 6.0, 60 °C, 6 h) | - α-amylase pretreatment improved LMW peptide (< 2 kDa) yield from 33.79 to 67.66% | Hong et al. (2021) |
Collagen (Skin) | Anti-aging of LWM peptides | - Produced by papain hydrolysis after formic acid and pepsin pretreatments (Hong et al. 2018) | In human dermal fibroblasts with ultraviolet A-exposure after treatment with the hydrolysate of 1 mg/mL - Increased cell viability (by 1.7 folds) - Reduced ROS generation (by 26%) - Increased type I α-procollagen production (by 1.5 folds) - Reduced MMP-1 (by 27) and MMP-9 (by 67%) synthesis - Reduced apoptotic genes (Bax and caspase-9) |