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Table 2 Bioactivities or functionalities of spent hen proteins (or derived peptides)

From: Conventional use and sustainable valorization of spent egg-laying hens as functional foods and biomaterials: A review

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
Fan et al. (2018), Gu et al. (2019)
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
Yu et al. (2018a, b)
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
Fan and Wu (2020), Fan et al. (2022)
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
Fan and Wu (2021a, b, c); Fan et al. (2021)
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)
Wang et al. (2019a, b)
  1. aProcessing condition includes enzymatical hydrolysis parameters (enzyme/substrate (E/S), temperature (T), and pH value)
  2. ABTS: 2,2ʹ-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); ACEi: angiotensin-converting enzyme (ACE) inhibitory; ACE2u, angiotensin-converting enzyme 2 (ACE2u) upregulating; DHE: dihydroethidium; DPPH: 2,2-diphenyl-1-picrylhydrazyl; FICA: ferrous ion chelating activity; FRAP: ferric reducing antioxidant power; ICAM-1: intracellular adhesion molecule-1; MMP: metalloprotease; LMW: low-molecular-weight; TNFα: tumor necrosis factor alpha; VCAM-1: vascular cell adhesion molecule-1