| Literature DB >> 35463462 |
Abstract
Spent hen are egg-laying hens reaching the end of their laying cycles; billions of spent hens are produced globally each year. Differences in people's attitudes towards spent hen as foods lead to their different fates among countries. While spent hens are consumed as raw or processed meat products in Asian countries such as China, India, Korea, and Thailand, they are treated as a byproduct or waste, not a food product, in the western society; they are instead disposed by burial, incineration, composting (as fertilizers), or rendering into animal feed and pet food, which either create little market value or cause animal welfare and environmental concerns. Despite being a waste, spent hen is a rich source of animal proteins and lipids, which are suitable starting materials for developing valorized products. This review discussed the conventional uses of spent hens, including food, animal feed, pet food, and compost, and the emerging uses, including biomaterials and functional food ingredients. These recent advances enable more sustainable utilization of spent hen, contributing to alternative solutions to its disposal while yielding residual value to the egg industry. Future research will continue to focus on the conversion of spent hen biomass into value-added products.Entities:
Keywords: Agricultural byproduct; Bioactive peptides; Biomaterials; Chicken; Functional foods; Spent hen; Sustainable utilization
Year: 2022 PMID: 35463462 PMCID: PMC9015908 DOI: 10.1186/s40643-022-00529-z
Source DB: PubMed Journal: Bioresour Bioprocess ISSN: 2197-4365
Fig. 1Profiles of egg and laying hen production. A Global egg production of 2008–2018. B Share of world market in egg production of global major producers in 2018. C Production of eggs (billions) and egg-laying hens (millions) of global major producers in 2018. Egg production was obtained from International Egg Commission; the number of spent hens were calculated based on the egg-laying capacity of 300 eggs/hen per year (Alders et al. 2018). D Body weight performance of several layer species. Body weight reference data of Bovans white, Lehmann brown, Lohmann Selected Leghorn (LSL), and Hy-Line W-36 referred to the management guide of New-Life Mills, Lohmann Breeders, and Ly-Line, respectively
Proximate composition, fatty acid and amino acid profiles of raw spent hen and meat
| Sample | Moisture (%) | Protein (%) | Fat (%) | Ash (%) | Fatty acid profile | Major amino acid | References |
|---|---|---|---|---|---|---|---|
| Spent hen carcassa | 59.8 | 18.5 | 14.9 | 5.3 | |||
| Whole spent henb | 58.2 | 17.9 | 19.1 | 4.5 | Glu, Gly, Asp, Leu, Arg, Pro, Lys | Freeman et al. ( | |
| Whole spent henc | 67.7 | 17.1 | 14.1 | 2.1 | Zubair ( | ||
| Whole spent hend | 60.1 | 21.4 | 16.3 | 2.2 | SFA (28%), MUFA (50%), PUFA (22%) | Safder et al. ( | |
| Spent hen breast meat | 72.0 | 22.9 | 1.5 | 1.5 | Glu, Leu, Arg, Lys, Asp | Okarini et al. ( | |
| Spent hen breast meat | 73.9 | 21.7 | 3.8 | 1.3 | SFA (38%), MUFA (33%), PUFA (29%) | Semwogerere et al. ( |
SFA saturated fatty acids, MUFA mono-unsaturated fatty acids, PUFA poly-unsaturated fatty acids
aSpent hen carcass (without feather, head, feet, and viscera), analyzed by our lab
bWhole spent hen (with feather)
cWhole spent hen (including skin, bone, muscle, leg, and gizzard)
dWhole spent hen (no indication on body components)
Fig. 2Protein extraction from spent hens. Protein extraction protocol 1 was summarized from Wang and Wu (2012) and Fan et al. (2021) with slight modifications; protein extraction protocol 2 was summarized from Zubair (2017) with slight modifications. Supernatants can be freeze-dried to obtain proteins, or be further dialyzed before collecting the retainates for freeze-drying
Bioactivities or functionalities of spent hen proteins (or derived peptides)
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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 ( |
| 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 ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| 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. ( |
| Collagen (Skin) | Anti-aging of LWM peptides | - Produced by papain hydrolysis after formic acid and pepsin pretreatments (Hong et al. | 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. ( |
aProcessing condition includes enzymatical hydrolysis parameters (enzyme/substrate (E/S), temperature (T), and pH value)
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
Biomaterial applications of spent hen proteins and lipids
| Proteins/lipids | Application (Products) | Processing conditions for preparing biomaterials | Product characterization | References |
|---|---|---|---|---|
| Muscle proteins | Wood adhesive | - Modified by 3% sodium dodecyl sulfate or 3 M urea | - The modification promoted protein unfolding, exposing more secondary structures that strengthen protein-wood bonding - Interaction between proteins and modification agents enhanced mechanical interlocking - The prepared adhesives can be applicable in both dry and wet environments | Wang and Wu ( |
| Muscle proteins | Bionanocomposite film | - Compression molding using glycerol (plasticizer), chitosan (cross-linker), and nanoclay (nanoparticles) | - The exfoliated bionanocomposite film had improved thermal, thermomechanical, and barrier properties, with possible uses as food packaging materials | Zubair et al. ( |
| Collagen (Gelatin) | Hydrogel | - Gelatin was made from extracted spent hen collagen - Gelatin scaffold was formed through crosslinking by adding glutaraldehyde | - Properties of gelatin scaffold: porosity (90%), pore size (range of 104–244 µm), and water uptake (1149%) - The scaffold promoted proliferation of human dermal fibroblasts for wound healing | Esparza et al. ( |
| Lipids | Plasticizer (Bio-epoxy) | - Lipids were extracted using supercritical CO2 - Bio-epoxy was produced by epoxidation of the extracted lipids | - Spent hen lipid-derived bio-epoxy materials were produced | Safder et al. ( |
| Lipids | Polymer precursor (ethenolysis) | - Ethenolysis was achieved by a microwave-assisted solvent-free approach with catalysts | - Spent hen lipids as a renewable lipidic source for ethenolysis | Pradhan et al. ( |
| Lipids | Bionanocomposite film | - Compression molding using spent hen-derived fatty acids and nanoclay | - Produced a lipid-based bionanocomposite film with enhanced thermal stability and flame retardancy compared to neat homopolymer | Safder et al. ( |
| Feather | Adsorbent | - Feather was functionalized with silver nanoparticles | - Enhanced adsorption capacity of rhodamine B by 30 folds | Azeez et al. ( |
| Feather | Adsorbent | - Treatment with hydrogen peroxide | - Effectively removed hazardous acid dye Amido Black 10B from aqueous solutions | Mittal et al. ( |
Fig. 3Overview of conventional and valorized uses of spent hens