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Sericin
Sericin
Sericin
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Sericin 1
Identifiers
OrganismBombyx mori
Symbolser1
UniProtP07856
Search for
StructuresSwiss-model
DomainsInterPro
Sericin 2
Identifiers
OrganismBombyx mori
Symbolser2
UniProtD2WL77
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StructuresSwiss-model
DomainsInterPro
Sericin 3
Identifiers
OrganismBombyx mori
Symbolser3
UniProtA8CEQ1
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StructuresSwiss-model
DomainsInterPro

Sericin is a protein created by Bombyx mori (silkworms) in the production of silk.[1] Silk is a fibre produced by the silkworm in production of its cocoon. It consists mainly of two proteins, fibroin and sericin. Silk consists of 70–80% fibroin and 20–30% sericin; fibroin being the structural center of the silk, and sericin being the gum coating the fibres and allowing them to stick to each other.[2]

Structure

[edit]

Sericin is composed of 18 different amino acids, of which 32% is serine. The secondary structure is usually a random coil, but it can also be easily converted into a β-sheet conformation, via repeated moisture absorption and mechanical stretching. The serine hydrogen bonds give its glue-like quality. The genes encoding sericin proteins have been sequenced. Its C-terminal part contains many serine-rich repeats.[3][4][5]

Using gamma ray examination, it was determined that sericin fibers are composed typically of three layers, all with fibers running in different patterns of directionality. The innermost layer, typically is composed of longitudinally running fibers, the middle layer is composed of cross fiber directional patterned fibers, and the outer layer consists of fiber directional fibers. The overall structure can also vary based on temperature, whereas the lower the temperature, there were typically more β-sheet conformations than random amorphous coils. There are also three different types of sericin, which make up the layers found on top of the fibroin. Sericin A, which is insoluble in water, is the outermost layer, and contains approximately 17% nitrogen, along with amino acids such as serine, threonine, aspartic acid, and glycine. Sericin B, composed the middle layer and is nearly the same as sericin A, but also contains tryptophan. Sericin C is the innermost layer, the layer that comes closest to and is adjacent to fibroin. Also insoluble in water, sericin C can be separated from the fibroin via the addition of a hot, weak acid. Sericin C also contains the amino acids present in B, along with the addition of proline.

Applications

[edit]

Sericin has also been used in medicine and cosmetics. Due to its elasticity and tensile strength, along with a natural affinity for keratin, sericin is primarily used in medicine for wound suturing. It also has a natural infection resistance, and is used variably due to excellent biocompatibility, and thus is used commonly as a wound coagulant as well.[6] When used in cosmetics, sericin has been found to improve skin elasticity and several anti-aging factors, including an anti-wrinkle property. This is done by minimizing water loss from the skin. To determine this, scientists ran several experimental procedures, including a hydroxyproline assay, impedance measurements, water loss from the epidermis and scanning electron microscopy to analyze the rigidity and dryness of the skin. The presence of sericin increases hydroxyproline in the stratum corneum, which in turn, decreases skin impedance, thus increasing skin moisture. Adding in pluronic and carbopol, two other ingredients that can be included in sericin gels, performs the action of repairing natural moisture factors (NMF), along with minimizing water loss and in turn, improving skin moisture.[2]

See also

[edit]

References

[edit]
Revisions and contributorsEdit on WikipediaRead on Wikipedia

Sericin

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from Grokipedia
Sericin is a hydrophilic, that constitutes 15–35% of the silkworm cocoon by weight, serving as the adhesive "gum" that coats and binds the inner fibroin filaments during cocoon formation. Extracted as a of the degumming process in the , it is primarily composed of polar , including serine (approximately 30–32 mol%), (16–20 mol%), (13–15 mol%), and , which contribute to its and bioactive potential. Structurally, sericin features a mix of random coils (dominant conformation) and β-sheets, with occasional α-helices and turns, resulting in a molecular weight range of 10–400 kDa that varies by extraction method and . Its physical properties include high water solubility (above 50°C), thermo-reversibility, and the ability to form hydrogels or films through β-sheet transitions, while chemically it is rich in hydroxyl, carboxyl, and amino groups that enable easy functionalization and crosslinking with other polymers. Biologically, sericin demonstrates , biodegradability (via enzymatic degradation), and multifaceted bioactivities such as effects (scavenging free radicals), action against like Staphylococcus aureus, anti-inflammatory responses, UV photoprotection, and promotion of and . Extraction of sericin typically involves thermal methods (e.g., boiling in water or solutions, yielding 17–23%), chemical treatments (acids, alkalis, or ), enzymatic (using proteases like alcalase for milder conditions), or advanced techniques like and microwaves to preserve bioactivity while minimizing environmental impact. These processes recover sericin from waste, turning an underutilized into a sustainable . In applications, sericin's versatility shines in , where it supports scaffolds for skin, bone, and nerve regeneration, as well as systems like nanoparticles and hydrogels for controlled release in cancer therapy and dressings. Beyond healthcare, it enhances through moisturizing (matching glycerol's hygroscopicity at low concentrations), (inhibiting by over 50% at 1%), and strengthening formulations. In industry, sericin improves textile dyeing, UV resistance, and for shelf-life extension, with emerging roles in sustainable plastics and treatments, underscoring its shift from waste to high-value .

Biological Origin

Sources

Sericin is primarily obtained as the outer layer protein coating the silk fibers within the cocoons produced by , accounting for 20-30% of the total cocoon weight. This protein forms a protective gum-like sheath around the inner core, derived exclusively from the silk glands of larvae during the pupation process. The domestic silkworm serves as the main source of sericin, with its cocoons yielding the highest commercial quantities due to widespread cultivation in . Wild silkworms, such as , also produce sericin, though in varying compositions compared to B. mori, and sericin is found across other Lepidopteran insects that spin cocoons. In the global industry, sericin emerges as a during the extraction of for raw production, with annual worldwide cocoon output exceeding 400,000 metric tons as of recent years. Major producers include and , which together account for over 90% of global supply, supporting a market valued at approximately USD 21 billion in 2025. This status positions sericin as an underutilized resource from the degumming process in . Sericin content varies significantly across silkworm species, with non-mulberry types like Antheraea assamensis exhibiting lower levels (around 15-20%) compared to B. mori's typical 25-30%, influenced by genetic differences. Environmental factors during larval rearing, such as temperature fluctuations (optimal at 25-28°C) and relative humidity (70-80%), further modulate yield by affecting silk gland activity and cocoon construction.

Role in Silk Production

Sericin is in the middle of the silkworm Bombyx mori during the final larval , where it is produced as a family of proteins encoded by genes such as Ser1 and Ser3. These proteins are secreted as an aqueous, gel-like solution that mixes with from the posterior , forming a viscous material essential for silk extrusion. This process enables the rapid production of sericin, which constitutes 20–30% of the cocoon's total weight, supporting the 's to up to 40% of the larva's body mass. During cocoon spinning, sericin functions as a hydrophilic gum-like that binds and coats the two filaments, enveloping them in multiple layers to form a cohesive thread approximately 900–1500 meters long. Secreted sequentially from distinct regions of the middle , sericin reduces between fibers and ensures structural integrity, allowing the to weave an intricate, layered cocoon structure. This coating is crucial for the thread's formation, as disruptions in sericin production, such as in mutants with truncated Ser1, result in defective, non-cohesive cocoons. The sericin layer provides critical protection to the within the cocoon by forming a barrier against environmental threats, including , microbial pathogens, and mechanical damage from predators. Its inherent properties, particularly in the outer cocoon layers, inhibit bacterial and fungal growth, while the overall cocoon architecture—reinforced by sericin—shields against and physical abrasion during . Additionally, sericin contributes to UV resistance, further enhancing pupal survival. In an evolutionary context, sericin plays a pivotal role in n insects, including B. mori, by enabling the encasement of the in durable, multi-layered cocoons that facilitate in diverse habitats. Highly divergent sericin genes across reflect adaptations for and protective functions, with duplications and sequence variations supporting the construction of species-specific silk structures beyond cocoons, such as larval feeding tubes. This conservation underscores sericin's fundamental contribution to silk-based pupal protection in the order .

Structure and Composition

Amino Acid Profile

Sericin, the glue-like protein coating silk in cocoons, comprises 18 distinct , with over 70% being polar or charged residues such as serine, , , and , which impart high hydrophilicity and solubility to the protein. Hydrophobic , including , , and , are present in low proportions, typically less than 3% each, contributing minimally to the overall structure. This composition distinguishes sericin from , which is dominated by smaller, non-polar residues like and . The most abundant amino acid in sericin is serine, accounting for 28–34% of the total residues, followed by (11–19%), (16–19%), and (6–12%), as determined across multiple analyses of cocoon extracts. These hydrophilic components, particularly the hydroxy-containing serine and , enable sericin's role in moisture retention and adhesion during cocoon formation.
Amino AcidApproximate Mole % (Range)Key Property
Serine (Ser)28–34Hydrophilic, hydroxyl
(Gly)11–19Polar, small
(Asp)16–19Charged, acidic
(Thr)6–12Hydrophilic, hydroxyl
(Glu)1–9Charged, acidic
(Ala)2–5Non-polar
(Lys)1–10Charged, basic
Representative composition from Bombyx mori sericin; values vary by layer and extraction method. Adapted from multiple studies. Sericin exists in three distinct layers around the core—A (outermost, protective), B (middle), and C (innermost, adherent)—each exhibiting subtle variations in profiles that reflect their functional gradients. These differences arise from spatially regulated in the silkworm's middle silk gland. Compared to , sericin from other silkworms like displays a shifted profile, with reduced serine (around 20–25%) but higher aspartic and glutamic acids (up to 25% combined), altering and adhesive properties. Extraction methods further influence integrity; alkaline boiling can hydrolyze up to 10–15% of sensitive residues like serine and threonine, while milder enzymatic or high-temperature water methods preserve the profile better, as shown in strain-specific studies. The profile is typically analyzed via acid followed by (HPLC) or automated amino acid analyzers, which quantify residues after derivatization for detection; these techniques ensure accurate molar percentages despite potential degradation during .

Molecular Structure

Sericin is a characterized by a predominantly conformation interspersed with β-sheet structures, lacking dominant α-helical elements. Its molecular weight varies widely from 10 to 400 kDa, influenced by the specific isoform and extraction conditions. This structural flexibility arises from the protein's composition, enabling its role as a hydrophilic in cocoons. In cocoons, sericin is organized into three distinct layers: the outermost A layer, which is the most hydrophilic and readily soluble in hot water; the middle B layer, with intermediate ; and the innermost C layer, which exhibits greater crystallinity and lower . These layers reflect differential deposition during silk production, contributing to the cocoon's protective properties. The protein features high proportions of β-turns and unordered regions, primarily due to its abundance of polar residues that promote hydrogen bonding and conformational disorder. These motifs enhance sericin's and amorphous character, distinguishing it from the more ordered core. techniques such as Fourier-transform infrared (FTIR) spectroscopy, (NMR), and (XRD) confirm sericin's largely amorphous nature, with FTIR and NMR revealing dominant and β-sheet signals, while XRD shows broad halos indicative of low crystallinity.

Properties

Physical Properties

Sericin demonstrates high in , particularly at elevated temperatures, reaching up to 95% dissolution at 90°C within 5 minutes, attributed to its abundance of polar residues such as serine and . This decreases at lower temperatures below 50°C, where sericin tends to form β-sheet structures and gels, while it remains insoluble in organic solvents like alcohols, ethers, acetone, and . is also -dependent, with an around 4.0; it is highly soluble in aqueous acidic solutions ( < 4) and alkaline conditions, but minimal near the . Thermally, sericin exhibits denaturation and gelation starting around 60–100°C, depending on concentration and extraction conditions, with high concentrations promoting gel formation through conformational transitions. Its thermal degradation occurs at higher temperatures of 210–220°C, as observed in thermogravimetric analysis, indicating reasonable stability for processing applications. Additionally, sericin shows UV resistance by absorbing UVC radiation and mitigating UVB-induced damage, enhancing its utility in protective materials. As of 2024, studies confirm sericin's UV absorption rate of approximately 65% at 280 nm. It is also biodegradable, readily broken down by proteolytic enzymes into peptides and amino acids in biological environments. In terms of rheological behavior, sericin forms viscous, shear-thinning solutions with an apparent viscosity of approximately 40 Pa·s, which is influenced by molecular weight—higher molecular weights (up to 400 kDa) increase viscosity due to greater chain entanglement. Surface properties stem from its amphiphilic nature, featuring both hydrophilic polar groups and hydrophobic domains, enabling the formation of emulsions and films suitable for coatings.

Biological Activities

Sericin exhibits a range of bioactive properties that contribute to its potential in health-related contexts, primarily stemming from its amino acid composition rich in polar residues. These activities include antioxidant, anti-inflammatory, antimicrobial, anticancer, neuroprotective, and moisturizing effects, often evaluated through in vitro and in vivo models. The antioxidant activity of sericin involves scavenging free radicals, attributed to its phenolic-like residues in and hydroxyl groups in . In DPPH assays, sericin demonstrates potent radical scavenging with IC50 values typically ranging from 0.07 to 0.4 mg/mL. This capacity helps mitigate oxidative stress in cellular models, such as fibroblasts exposed to reactive oxygen species. Sericin's anti-inflammatory effects are mediated by inhibition of pro-inflammatory cytokines, including TNF-α and IL-6, in lipopolysaccharide-stimulated macrophages and animal models of inflammation. For instance, sericin treatment significantly reduces TNF-α and IL-6 levels in serum of stressed rodents, promoting resolution of inflammatory responses. Additionally, it enhances wound healing by stimulating fibroblast proliferation and collagen deposition in rat models. Antimicrobial properties of sericin arise from its charged and polar residues, which disrupt bacterial and fungal cell membranes. It shows efficacy against Gram-positive bacteria like Staphylococcus aureus, with inhibition zones comparable to standard antibiotics in disc diffusion assays, and extends to Gram-negative strains such as Escherichia coli and fungi like Candida albicans. Beyond these, sericin induces apoptosis in cancer cell lines, such as breast and colon cancer cells, via pro-oxidative stress mechanisms that elevate reactive oxygen species and activate caspase pathways. In dietary supplementation studies on mice with colon tumors, sericin reduced the incidence of colonic adenomas by 62%. Its neuroprotective role involves alleviating oxidative stress and neuroinflammation in neuronal models, protecting against damage in diabetic neuropathy and sleep deprivation-induced impairment by restoring antioxidant enzyme levels and BDNF expression. Sericin also promotes skin moisturization by enhancing epidermal hydration and filaggrin expression in topical applications. Overall, these activities are largely driven by the hydroxyl groups in serine and tyrosine residues, which facilitate interactions with biological targets and enhance bioavailability through sericin's inherent solubility in aqueous environments.

Extraction Methods

Traditional Extraction

The degumming process, which removes the outer gum layer from cocoons to obtain fibroin fibers, originated alongside sericulture in ancient China around 2700 BCE and evolved into standardized industrial methods by the 19th century in Europe, particularly in silk-reeling centers like . These early techniques developed into more systematic approaches for isolating sericin as a byproduct. The primary conventional method for isolating sericin is the degumming process, which involves boiling silk cocoons in water or dilute alkaline solutions to solubilize and remove the sericin coating, leveraging its natural solubility in hot water. A common approach uses 0.5% sodium carbonate (Na₂CO₃) solution at 90-100°C for 1-2 hours, typically yielding 20-30% sericin recovery relative to the cocoon's weight, as silk cocoons naturally contain this proportion of sericin. Another traditional technique is acid hydrolysis, employing acids such as hydrochloric acid (HCl) or formic acid to achieve complete sericin breakdown by cleaving peptide bonds. However, this method often results in degraded protein fragments with reduced molecular weight and altered structure, limiting its utility for preserving sericin's native properties. These historical methods, while effective for sericin isolation, present notable limitations, including high energy consumption due to elevated temperatures and prolonged boiling, environmental pollution from alkaline wastewater effluents, and partial denaturation of the sericin protein during processing.

Advanced Techniques

Advanced techniques for sericin extraction emphasize eco-friendly, low-impact processes that minimize chemical use while preserving the protein's native structure, molecular weight, and bioactivity, such as antioxidant and moisturizing properties. These methods leverage physical, enzymatic, or biological mechanisms to achieve high recovery rates (often exceeding 90%) and purity levels up to 95%, reducing environmental pollution from traditional degumming wastewater. Enzymatic extraction employs proteases like alcalase or to selectively hydrolyze sericin during degumming, operating under mild conditions to limit degradation of the silk fibroin core. Alcalase, a bacterial subtilisin-type protease, is typically applied at pH 8.0–9.0 and 50–60°C for 1–2 hours, yielding over 90% sericin recovery with molecular weights retained above 100 kDa and minimal fibroin damage. , effective at neutral pH 7.0–8.0 and 40–50°C, achieves similar efficiencies (85–95% sericin removal) but requires longer incubation (up to 24 hours) for complete hydrolysis without altering sericin's bioactive peptides. These approaches outperform chemical methods by preserving sericin's amphiphilic and antioxidant functionalities, as evidenced by higher soluble protein yields (up to 4 times that of untreated controls). High-pressure and ultrasound-assisted methods disrupt sericin-fibroin bonds through mechanical forces, accelerating extraction while cutting processing time and chemical inputs by 50–70%. Steam explosion, a high-pressure technique, applies 120–150°C under 2–5 atm for 10–30 minutes, achieving 85–95% sericin release by swelling and fracturing cocoon structures without solvents. Ultrasound-assisted extraction uses sonication at 20–40 kHz for 20–40 minutes, often combined with water or mild buffers, to generate cavitation bubbles that enhance sericin solubility and yield up to 92%, while maintaining β-sheet conformations for bioactivity. These techniques reduce energy consumption (e.g., ultrasound halves traditional boiling times) and produce sericin with uniform molecular weights (20–400 kDa), ideal for downstream biomedical uses. As of 2025, optimized green ultrasound methods with pretreatment have further improved water-based extraction, achieving high yields while remaining chemical-free. Biological methods utilize microbial fermentation or green solvents for sustainable, enzyme-mediated isolation of sericin, promoting zero-waste sericulture by valorizing byproducts. Fermentation with Bacillus subtilis employs submerged cultures at pH 7.0–8.0 and 30–37°C for 24–48 hours, where secreted subtilisin-like proteases degrade sericin, yielding 80–90% recovery and hydrolysates rich in bioactive peptides (e.g., antioxidant activity >1500 μmol TE/L). This process integrates with agro-industrial wastes as substrates, enhancing scalability and reducing costs by 30–40% compared to pure enzyme systems. Ionic liquids, such as 1-butyl-3-methylimidazolium chloride (BMIM.Cl) in aqueous solutions (10–20% v/v), facilitate eco-friendly degumming at 25–50°C for 1–4 hours, extracting 85–95% sericin from both mulberry and non-mulberry silks with preserved secondary structures (confirmed by FTIR) and no fiber damage. These solvents are recyclable, minimizing environmental impact while enabling high-purity isolation (>90%). Supercritical CO₂ extraction, conducted at 95–127°C and 150–400 for 45–70 minutes following mild acid pretreatment, removes 95–98% sericin solvent-free, preserving native conformations and supporting sustainable by recycling CO₂. Microwave-assisted extraction irradiates cocoons at 400–800 W for 5–15 minutes in , yielding up to 99.8% sericin via rapid volumetric heating that disrupts bonds without chemicals, halving use and enabling zero-waste processes. Recent chemical-free methods using only and , optimized as of 2025, achieve sericin yields of 9–18% under controlled conditions, further reducing environmental impact. These innovations reduce by 80% and align with principles, as demonstrated in pilot-scale trials.

Applications

Biomedical Uses

Sericin has garnered significant attention in dressings and due to its , , and properties, which promote regeneration and accelerate processes. In preclinical studies, sericin-based scaffolds, such as hydrogels and nanofibers combined with silk fibroin, have demonstrated enhanced re-epithelialization, deposition, and reduced scar formation in diabetic models. For instance, a prospective involving 40 patients with diabetic foot ulcers showed that fibroin-aloe gel films led to notable improvements in closure rates compared to controls, highlighting its potential for clinical translation in managing chronic wounds like diabetic ulcers. In systems, sericin's pH-responsive swelling and chemical reactivity enable the development of nanoparticles, hydrogels, and films for controlled release of therapeutic agents. These formulations have been effective in encapsulating antibiotics for applications, reducing bacterial loads in wound sites—such as sericin-silver nanoparticles with in scaffolds that significantly inhibited and growth (p < 0.05). For anticancer therapy, sericin-based carriers like ZIF-8@@sericin nanoparticles achieved up to 92% drug release in acidic tumor environments, enhancing in colorectal and cells via pathways including and PI3K/Akt. Sericin finds applications in and , leveraging its moisturizing and capabilities to formulate products like lotions, creams, and films. Hydrolyzed sericin at 0.01% w/w in skin lotions has shown stability and enhanced hydration without irritation in patch tests on 24 volunteers, promoting barrier function and reducing for anti-aging effects. Its ability to inhibit UVB-induced damage further supports use in UV-protective formulations, improving elasticity and pigmentation control in dermatological treatments for conditions like and . Emerging from 2020 to 2025 has explored sericin in neuroprotective implants and advanced anticancer delivery, building on its bioactivities for therapeutic innovation. In nerve regeneration models, sericin scaffolds promoted functional recovery in 10 mm defects by supporting axonal growth and reducing inflammation. For , oral sericin administration (100–300 mg/kg) mitigated deprivation-induced impairment in mice by upregulating synaptic proteins like PSD-95 and suppressing markers such as MDA. Anticancer applications include sericin nanoparticles for targeted siRNA and drug co-delivery, inhibiting tumor growth in preclinical models.

Industrial and Other Uses

Sericin finds extensive application in the as a natural sizing agent and finishing material, enhancing the dyeability and mechanical properties of various fabrics. For instance, treatment with 0.5% sericin combined with 4% improves the dye absorption of fabrics, facilitating more efficient and eco-friendly reactive processes. Additionally, sericin finishes impart wrinkle resistance to and textiles by increasing the wrinkle recovery angle, thereby improving fabric durability and appearance without synthetic chemicals. In wool processing, sericin enhances fabric softness, moisture absorption, and UV protection when complexed with metal ions, while its use as a biodegradable alternative to synthetic sizes contributes to reduced consumption in . In the food sector, sericin is utilized to create edible films and coatings that extend the of perishable items through its film-forming capabilities. Blends of sericin with and form transparent films applied to , such as tomatoes, which maintain freshness for up to one additional week compared to uncoated samples. These coatings leverage sericin's inherent properties to provide a barrier against microbial growth and moisture loss, promoting solutions. Furthermore, sericin serves as an additive in supplements, where low concentrations (e.g., 0.1%) enhance the mechanical strength of protein-based foods like products. Environmental applications of sericin include its role in developing biodegradable plastics and as an adsorbent for . Sericin-based composites contribute to eco-friendly plastics, with current global production at approximately 0.05 million tons annually and potential to capture up to 10% of the 400 million-ton conventional plastics market, thereby reducing pollution from textile waste. In , sericin-derived materials, such as hierarchical porous structures, achieve over 99% adsorption efficiency for like lead (Pb(II)) within 15 minutes, enabling effective removal from industrial effluents. Beyond these sectors, sericin is employed in non-biomedical , particularly as a in shampoos and moisturizers at concentrations of 0.02% to 20%, where 3% sericin provides hydration equivalent to 60% , improving elasticity and shine. In , sericin coatings on promote rates and early growth by enhancing retention and nutrient delivery. The global sericin market, driven by these diverse industrial demands, is projected to reach USD 361.5 million by 2025, reflecting steady growth at a compound annual rate of 5.8%.

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