Silk Sericin Protein Materials: Characteristics and Applications in Food-Sector Industries
Abstract
:1. Introduction
2. Sericin: Extraction Process and Characteristics
3. Physicochemical Characteristics of Sericin
3.1. Amino Acid Composition
3.2. The Fourier-Transform Infrared Spectroscopy (FTIR) Analysis of Sericin
3.3. Coloration
3.4. Molecular Weight Determination
3.5. Elemental Composition of Sericin
3.6. Absorption Spectra of Sericin
4. Application of Sericin in Food-Sector Industries
4.1. As a Food-Packaging and Food-Coating Material
Limitation | The Supplements Used with Sericin | References | |
---|---|---|---|
Sericin-based food-packaging materials | The weak mechanical properties promoted the sericin self-aggregation | Nanocellulose can also be used to strengthen a sericin film’s limit regarding its insufficient physical qualities, such as bamboo-derived cellulose nanofibrils. | [71] |
Using sericin in combination with other biopolymers can minimize the permeability of the films by lowering the amount of plasticizer to maintain flexibility. | [70] | ||
Chemical crosslinking reaction between sericin and glucose helps to overcome sericin film’s limitations, such as water resistance and mechanical properties. | [69] | ||
Glycine together with sericin generates a synergistic action with the water molecule on the sericin film, thereby increasing the elasticity, moisture level, and β-sheet structure of the sericin film moderately. | [75] | ||
Sericin/agarose film bonded with Ag/ZnO not only improves the mechanical properties of sericin but also has excellent antibacterial performance. | [76] | ||
Hydrophilicity-it is delicate in a water environment | Sericin film added with hydrolysate increases the water vapor permeability. | [74] | |
Sericin films incorporated with glucomannan have greater solubility combined with glycerol; thus, sericin has a flexible functionality without raising the film’s water vapor permeability. | [70] | ||
Preservation | The sericin-based edible coating material, including chitosan, aloe vera, and glycerol, has the potential to prolong the storage life of tomatoes under storage at 25 °C and relative humidity of 70%. | [21] | |
By applying glucose to create a sericin coating, food oxidation can be controlled and the shelf life lengthened. | [69] |
4.2. Other Food Applications of Sericin
4.3. Challenges and Benefits of Using Silk Sericin Protein Materials in Food Products
5. Other Potential Applications of Sericin
5.1. As an Antibacterial Agent
5.2. Antioxidant Potential of Sericin
5.3. Anticancer Potential of Sericin
5.4. Anti-Tyrosinase Potential of Sericin
5.5. Anti-Inflammatory Potential of Sericin
5.6. Anti-Aging Potential of Sericin
5.7. Other Potentials of Sericin
Biological Properties | Target | Influence | References |
---|---|---|---|
Antibacterial activity | - Sericin promotes the blebbing of bacterial cell membranes, thus preventing the growth and reproduction of bacteria. | Sericin purity and extraction process. | [97] |
- Micrococcus luteus exhibits its antibacterial characteristics through its impregnated layers. | Sodium carbonate in the density of 10 mg/mL. | [32] | |
- Sericin inhibits the growth of E. coli and S. aureus. | - Sericin extracted for 90 min in hot-water methods at 30 μg; - Sericin extracted for 60 min in Na2CO3 methods at 40 μg. | [93] | |
- Pathogen-specific response of the polypeptide (E. coli, B. cereus, S. aureus, K. pneumoniae, and P. aeruginosa) may be due to phagocytosis. | The extracted sericin using physical methods at 50 mg. | [95] | |
- Sericin suppresses bacteria’s metabolism, formation of cell walls, peptides that bind to lipopolysaccharides, and protein folding (E. coli, S. aureus, Vibrio cholera, Salmonella typhi, and Shigella flexneri). | Sericin was extracted using sodium chloride and ethanol at different concentrations (25, 50, 75, and 100 mL). | [94] | |
- Sericin has the potential for antibacterial activity due to its combination with other antibacterial bioactive molecules. | The peptide of Sericin under 29 kDa. | [96] | |
Antioxidant activity | - Alanine and glycine have intracellular antioxidant properties; - Mitochondrial structural preservation through the control of prohibitin-2, mitochondrial elongation factor Tu, and NADH-ubiquinone oxidoreductase, intracellular proteins that control apoptosis and autophagy. | Its purity and extraction process. | [12] |
- Sericin can protect against oxidative stress and decrease reactive oxygen species. | Its purity and extraction process. | [98] | |
- By using the DPPH and ABTs assay to diminish the size of sericin, its antioxidant activity might be increased. | The extraction time has changed (15, 30, 60, 90, and 120 min), | [101] | |
- Sericin might be the prevention of a chain reaction carried on by free radicals. | Male mice were given at different concentrations (0.375, 0.75, and 1.50 g/kg b.w.). | [99] | |
- Sericin has an antioxidant activity that reacts with free radicals to turn them into more stable molecules and stop the chain reaction from starting. | Using samples of pure sericin (A1) and crude sericin extracts (A2 and A3) at concentrations ranging from 5 to 60 mg/mL. | [44] | |
- The scavenger activity increased as a result of its reduction in size. | The bacterial-purified protease. | [100] | |
- The antioxidant defense system against ROS elements includes glutathione (GSH), superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx). | Various extraction methods (conventional, autoclaving, urea degradation, alkali degradation, and acid degradation) and silk-cocoon varieties. | [43] | |
- Sericin substantially decreases intracellular ROS shown on fluorescence; - It has been hypothesized that sericin’s primary amino acids protect B. mori’s hemocytes and midgut epithelial cells against oxidative damage, most likely because of sericin’s ability to scavenge ROS; - The polyphenols and flavonoids in sericin are what give it its antioxidant qualities. | Its purity and extraction process. | [18] | |
- Sericin’s high serine and threonine concentrations, as well as its 40% hydroxyl content, act as antioxidants by chelating trace metals such as copper and iron. | Amounts of 0.0%, 0.5%, and 1.0% sericin. | [35] | |
- 10 μg/mL of sericin from Bombyx mori shows 50% of DPPH radical scavenging; - When the sericin concentration increased, the amount of radical scavenging activity also did in a dose-dependent manner. | Amounts of 10, 20, 40, 80, and 100 μg/mL of silk sericin. | [117] | |
Anticancer activity | - Silk sericin based self-assembled nanoparticles stimulates apoptosis in the MCF-7 breast cancer cells. | The method of sericin isolation and the families of the silk cocoon. | [103] |
- Cancer cells, such as breast, colon, colorectal, lung, cervical, and prostate cancer cells, treated with sericin show decreasing viability owing to increasing the concentration of sericin. | Sericin from Antheraea assamensis, Bombyx mori, and Philosamia ricini was measured at 0.5, 1.0, 2.0, and 4.0 mg/mL. | [102] | |
- The reduction of Bcl-2, which is a regulatory factor that promotes or inhibits apoptosis, and increased activity of caspase-3, which is an active factor in the end process of apoptosis, stimulate the apoptosis of colon cancer cells; - Sericin damages cancer cells, causes morphological changes, encourages cell shrinkage, and induces nuclear condensation. | Amounts of 0, 0.25, 0.50, 0.75, and 1.0 mg/mL of sericin. | [94] | |
- Sericin shows the reduction effect of the 1,2-dimethylhydrazine agents, which is a cancer-growth promoter. | Sericin hydrolysis by using chemical, thermal, or physical extraction processes. | [1] | |
- Sericin significantly suppressed the proliferation of triple-negative breast cancer (TNBC), which is known to be difficult to treat and has a severe prognosis and advanced cell apoptosis by inhibiting the signaling pathway, such as PI3K/Akt. | Amounts of 0, 0.5, 1.0, 2.0, 4.0, 8.0, and 16.0 mg/mL of sericin. | [104] | |
- Sericin is considerately effective on SW480 cells, which are isolated from colorectal cancer as the inhibitory since it seems to decrease their viability and induce apoptosis. | Sericin of various sizes and concentrations (ranging from 25 to 1600 mg/mL) | [105] | |
- Sericin has properties for cancer inhibitory, such as human lung, cervical, and prostate cancer, by inducing apoptosis and cell-cycle arrest. | Amounts of 0.2, 0.3, 1.0, 1.5, 3.0, 5.0, and 10.0 μg/μL of sericin. | [106] | |
Anti-tyrosinase activity | - The flavonoids and carotenoids which are accumulated in sericin layers were caused to endow sericin with anti-tyrosinase activity. | Its purity and extraction process. | [14,18] |
- Sericin inhibits the tyrosinase enzyme. | Basin, deflossing, and reeling waste of sericin. | [19] | |
- Sericin has anti-tyrosinase properties of various biological functions that suppress polyphenol oxidase. | Amounts of 0%, 0.5%, and 1.0% of sericin | [15,35] | |
- Sericin has extracted the highest value of an anti-tyrosinase activity is sericin with urea; - The large amounts of arginine and valine, which are bound with tyrosinase enzyme extracted from the extraction process with urea, could increase anti-tyrosinase activity. | - Sericin from various extraction methods (heat, urea, acid, and base); - Enzymatic digestion, denaturing agents (boiling with detergents, alkaline chemicals, and chaotropic agents), polymeric membranes, infrared radiation, steam, ultrafiltration, and nanofiltration (autoclave). | [55,100] | |
- Sericin has the potential to inhibit fruit and vegetable enzymatic browning. | An 8% (w/v) sericin solution. | [39] | |
- Arginine enhances the anti-tyrosinase activity of sericin because it could be bounded and inhibited with tyrosinase enzymes; - Hydrophobic amino acids, such as valine, alanine, and leucine, have the anti-browning properties of SH due to the metal-chelating abilities of amino acids because they are bounded with hydrophobic pockets near the tyrosinase enzyme. | Amounts of 5, 10, and 20 μg/mL of sericin. | [84,107] | |
Anti-inflammatory activity | - Inducible Nitric Oxide Synthase (iNOS) and Cyclooxygenase-2 (COX-2) genes attributed to inflammatory gene expression are down-regulated by treatment with sericin dose-dependently; - Silk sericin in vivo not only inhibits carrageenan-induced inflammation due to the activation of anti-inflammatory reactions but also regulates the production of cytokines as pro-inflammatory. | Amounts of 0.25, 0.5, 1.0, and 2.0 mg/mL of sericin. | [109] |
- Gel formulations containing silk sericin obtained from both a natural source and alginate may be the treatment of inflammation in suppressing carrageenan-induced inflammation. | Amounts of 20% and 80% sericin-loaded alginate nanoparticle gel. | [110] | |
- Expression of mRNA by human peripheral blood mononuclear cells and production of pro-inflammatory cytokines (TNF-α, IL-6, IL-23, and IL-12p40) were reduced when silk sericin and naringin were combined. | Naringin (20 g/mL) and sericin (100 g/mL) combined in a 1:1 ratio (v:v). | [111] | |
- Silk sericin grafted with phenolic compounds such as hydroquinone and pyrogallol has significant anti-inflammatory properties; - Sericin-phenolic conjugates were effective to inhibit 15-LOX activity. | The supernatant was mixed with hydroquinone and pyrogallol in a 1:10 (phenol/sericin) ratio. | [108] | |
Anti-aging activity | - Sericin inhibits apoptosis and stimulates collagen type I synthesis; - Sericin regulates nitrite, which causes oxidative stress and the development of b-cell lymphoma 2 (bcl-2), is increased. | - 500 μg/mL of sericin; - Days 1, 3, 5, 7, 9, and 11. | [115] |
-Sericin can restore natural moisturizing factors and stimulate moisturizing properties. | Sericin hydrolysis by using chemical, thermal, or physical extraction processes. | [112] | |
- Sericin inhibits apoptosis in UVB (30 mJ/cm2)-irradiated human epidermal keratinocyte cells and prevent the activation of caspase-3. | Sericin hydrolysis by using chemical, thermal, or physical extraction processes. | [114] | |
- In the sericin group, five animals (83.33%) had significant collagen deposition, fibrosis, and fibroblastic activity. | Wistar albino adult male rats weighing between 257 to 395 g were given 30 mg of sericin powder through their thoraxes at the age of 12 weeks. | [113] |
6. Conclusions and Future Prospects
Funding
Acknowledgments
Conflicts of Interest
References
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Methods | Advantages | Limitations | Reference(s) | |
---|---|---|---|---|
Physical | Hot water | - It is to use natural polymers. | - The purity of sericin was low; - The limited information about the composition. | [29,30] |
Chemical | Alkaline solution: Na2CO3 (dialysis sericin solution containing alkaline or acidic solutions) | - It is low-cost to use on a large scale; - It has good high yield and antioxidant activity. | - Separate ions and molecules in the sericin solution; - Exchange with ions and other molecules. | [3,31,32] |
Alkaline property: Marseille soap | - The soap is a natural material. | - Marseille soap separation is very difficult; - The soap is very expensive. | [3,33] | |
CaCl2 (Calcium chloride) | - Recover the high-purity sericin from the silk cocoon; - Decrease the amount of microbic waste. | - The dialysis process is essential. | [29] | |
Enzymatic | A protease enzyme | - DPPH radical-scavenging activity and a three-fold higher total essential amino acid value than the water-extraction method. | - It is expensive to use in large quantities. | [33] |
Alanine | Arginine | Aspartic acid | Glutamic acid | Glycine | Histidine | Isoleucine | Leucine | Lysine | Methionine | Phenylalanine | Serine | Threonine | Tryptophan | Tyrosine | Proline | Valine | Reference |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
6.47 | 9.75 | 3.82 | 6.90 | 12.24 | 3.50 | 4.23 | 2.85 | 4.76 | 1.56 | 7.89 | 7.01 | 7.24 | 6.36 | 8.58 | NA | 6.88 | [31] |
5.71 | 4.45 | NA | NA | 12.17 | 0 | 1.48 | 2.03 | 0.6 | 0 | NA | 32.55 | 7.48 | NA | 3.69 | 2.38 | 6.31 | [29] |
3.28 | 4.71 | 11.52 | 2.92 | 12.6 | 2.05 | 0.34 | 1.05 | 2.33 | 0.13 | 0.53 | 40.51 | 8.45 | NA | 5.42 | 0.59 | 3.56 | [19] |
4.1 | 2.87 | 15.64 | 4.61 | 15.03 | NA | 0.56 | 1 | 2.35 | 3.39 | 0.28 | 33.63 | 8.16 | NA | 3.45 | 0.54 | 2.88 | [34] |
5.3 | 1.8 | 18 | 4.6 | 15.7 | 1.3 | 0.7 | 1.1 | 2.5 | <0.05 | 0.4 | 32.2 | 8.4 | NA | 3.7 | 0.6 | 3.6 | [18] |
3.8 | 3.9 | 17.8 | 4.4 | 19.1 | 1 | 0.4 | 0.8 | 2.7 | <0.05 | 0.2 | 31 | 8 | NA | 3.3 | 0.4 | 3.1 | [35] |
NA | 5~15 | 7~10 | 4~6 | 10~20 | 3~6 | NA | NA | 20~30 | NA | NA | 7~16 | 3~10 | NA | 4~6 | NA | NA | [24] |
4.6 | 2.8 | 19.1 | 4.1 | 12.2 | 0.9 | 1.4 | 0.6 | 10.2 | <0.05 | 0.4 | 30.4 | 6 | NA | 3.8 | 0.8 | 2.6 | [37] |
6 | 3.1 | 16.7 | 4.4 | 13.5 | 1.3 | 0.7 | 1.1 | 3.3 | 0.04 | 0.5 | 33.4 | 9.7 | 0.2 | 2.6 | 0.7 | 2.8 | [38] |
4.6 | 2.8 | 19.1 | 4.1 | 12.2 | 0.9 | 1.4 | 0.6 | 10.2 | <0.05 | 0.4 | 30.4 | 6 | NA | 3.8 | 0.8 | 2.6 | [36] |
4.3 | 4.9 | 18.8 | 7.2 | 10.7 | 1.7 | 1.3 | 1.7 | 2.1 | 0.5 | 1.6 | 27.3 | 7.5 | 0.4 | NA | 1.2 | 3.8 | [39] |
NA | 11.95 | 14 | 3.3 | 23.2 | 1.13 | 0.91 | 2.08 | 3.18 | 0.77 | 1.29 | 21.56 | 7.04 | NA | 6.23 | NA | 3.36 | [40] |
Amino Acid | Extraction Method of SS | |||
---|---|---|---|---|
Heat | Urea | Acid | Alkaline | |
Asp | 15.64 | 18.31 | 15.93 | 19.88 |
Ser | 33.63 | 31.27 | 31.86 | 30.01 |
Glu | 4.61 | 5.27 | 5.75 | 5.93 |
Gly | 15.03 | 11.23 | 10.49 | 11.01 |
His | 1.06 | 3.26 | 2.47 | 1.72 |
Arg | 2.87 | 5.41 | 4.92 | 4.92 |
Thr | 8.16 | 8.36 | 8.51 | 6.49 |
Ala | 4.10 | 4.33 | 3.72 | 4.21 |
Pro | 0.54 | 1.46 | 0.78 | 1.24 |
Cys | 0.54 | 0.39 | 0.53 | 0.23 |
Tyr | 3.45 | 0.36 | 5.56 | 5.24 |
Val | 2.88 | 2.96 | 2.95 | 2.94 |
Met | 3.39 | 0.12 | 0.06 | 0.15 |
Lys | 2.35 | 3.14 | 3.48 | 2.89 |
Ile | 0.56 | 0.96 | 0.87 | 0.75 |
Leu | 1.00 | 1.58 | 1.43 | 1.56 |
Phe | 0.28 | 0.60 | 0.71 | 0.81 |
The Raw Material | Identification Data | How to Get It |
---|---|---|
Sericin | Batch: S1911251 | From the supplier 1 |
Bovine lactoferrin | Batch: 107CLXP | From the supplier 2 |
Chicory inulin 3 | Batch: RHBGD1BGD1 | Purchased from local trade 4 |
Citrus pectin | Batch: 5999884818779 | Purchased from local trade 4 |
Stevia | Batch: 8 | Purchased from local trade 5 |
Apple juice (depectinized) | Batch: Bm 095-22 | Purchased from local trade 6 |
Agar–agar | Batch: 210040401 | Purchased from local trade 7 |
Lemon | - | Purchased from local trade |
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Seo, S.-J.; Das, G.; Shin, H.-S.; Patra, J.K. Silk Sericin Protein Materials: Characteristics and Applications in Food-Sector Industries. Int. J. Mol. Sci. 2023, 24, 4951. https://doi.org/10.3390/ijms24054951
Seo S-J, Das G, Shin H-S, Patra JK. Silk Sericin Protein Materials: Characteristics and Applications in Food-Sector Industries. International Journal of Molecular Sciences. 2023; 24(5):4951. https://doi.org/10.3390/ijms24054951
Chicago/Turabian StyleSeo, Su-Jin, Gitishree Das, Han-Seung Shin, and Jayanta Kumar Patra. 2023. "Silk Sericin Protein Materials: Characteristics and Applications in Food-Sector Industries" International Journal of Molecular Sciences 24, no. 5: 4951. https://doi.org/10.3390/ijms24054951
APA StyleSeo, S. -J., Das, G., Shin, H. -S., & Patra, J. K. (2023). Silk Sericin Protein Materials: Characteristics and Applications in Food-Sector Industries. International Journal of Molecular Sciences, 24(5), 4951. https://doi.org/10.3390/ijms24054951