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The main objective of this research is to synthesize silk sericin and silk sericin powder for turbidity removal of synthetic turbid water. Silk sericin used as coagulant aid in this study was extracted from silk cocoons by boiling them with 0.5% (w/w) Na2CO3solution at 90°C for 60 min. Synthetic turbid water with the initial turbidity of about 50 NTU, 75 NTU, and 100 NTU, the turbidity removal efficiencies 89.2±5.41%, 90±3.48% and 87±4.31% respectively. For the powder silk sericin, the turbidity removal efficiencies 96±0.77%, 88±2%, and 96±1.73% respectively. Introduction

Silk sericin has been recently investigated for many biological roles. This study aimed to develop the new delivery system to control the release of silk sericin. The alginate microparticles encapsulating silk sericin were fabricated by electrospraying technique. Concentrations of silk sericin and alginate polyelectrolyte solutions were investigated. All microparticles had an average size of 264–284 μm and could entrap silk sericin with high entrapment efficiency (84–89%). The microparticles could deliver silk sericin in a rate-controlled manner. This study would show a promising controlled release application of silk sericin protein from alginate microparticles fabricated by the means of electrostatic forces.

In this study, the effect of sericin on synthesis of the silica was investigated. Using the mixture of sericin solution and tetraethyl orthosilicate (TEOS), it was confirmed that silica could be synthesized in the presence of sericin, which was verified by thermal gravimetric analysis (TGA), Fourier-transformed infrared spectrometer (FT-IR) and nuclear magnetic resonance spectrometer (NMR) analysis. The TGA and FT-IR data revealed that silica-sericin complex was formed as a final product. Based on the TGA result, the content of silica and sericin in the complex would be 87 and 13%, respectively. The degree of silica condensation was higher than the natural biosilica. It could be concluded that sericin can induce the synthesis of silica directly from TEOS, which is similar to silicatein from marine sponges.

Recently, silk sericin has attracted the attention of researchers owing to its useful properties as a biomaterial including 1) good wound healing and cell activities, 2) fast gelation character, and 3) high water retention property. In the present study, silk sericin was prepared using different extraction times in hot water and the effect of extraction time on the rheological properties of sericin solutions and gels was examined. It was found that the production yield of sericin increased with extraction time. The shear viscosity of sericin solutions and gels decreased with increasing extraction time due to a decrease in sericin molecular weight. When the sericin solution transformed to a gel, the viscosity increased and the shear thinning behavior was more evident. In addition, the shear stress measurements indicated that the slip between the sericin samples and the measuring plate of the rheometer was increased by the gelation of sericin. The compression strength of sericin gel could be increased remarkably (by more than 100 fold) by preparation using the freezing and thawing method.

Sericin is usually abandoned after the degumming process. However, it could be a valuable bioresource if an economically efficient recovery process could be set up. In this study, sericin was recovered directly from the degummed waste solution by adding calcium chloride, which induced the precipitation of the surfactant, sodium oleate, by charge interaction. The recovery yield was maximum when 10% of calcium chloride was added. Further increase in the calcium chloride concentration induced the precipitation of sericin. The recovered sericin had a molecular weight distribution similar to that of the hot-water-extracted sericin; but some highmolecular- weight sericin could not be recovered. The secondary structure and amino acid composition of the recovered sericin were similar to those of conventional hot-water-extracted sericin. We expect that sericin recovered from the degummed waste solution could be an alternative to the hot-water-extracted sericin, which is widely used in various applications.

Silk sericin (SS) has been fabricated into beads using a 1 M LiCl/DMSO solvent and utilized as a heavy metal adsorbent. Among the various heavy metals, we targeted Cr(VI) for adsorption using SS beads and found that its adsorption depended on the coagulant used for the fabrication of the SS beads. When methanol was used as a coagulant, the beads had a better adsorption capacity than when ethanol was used except at pH 1. The adsorption behavior of Cr(VI) on the SS beads followed the BET isotherm. The maximum adsorption capacity was 33.76 mg/g at pH 2. The adsorption of Cr(VI) was confirmed by FT-IR and EDS analyses. Finally, the desorption was carried out using NaOH solution, and it was found that 73.19% of the adsorbed Cr(VI) could be detached.

In recent years, the use of stimuli-sensitive interpenetrating polymer network (IPN) hydrogels for the encapsulation and controlled release of protein drugs has received significant attention. The purpose of the present study was to investigate the release of bovine serum albumin (BSA), a model drug, from a series of thermosensitive silk sericin (SS) poly(N-isopropylacrylamide) and pH-responsive SS poly(methacrylic acid) IPN hydrogels. The effect of the chemical architecture of the IPN was investigated on the percentage loading of BSA and its subsequent release from the loaded devices. The temperature and pH of the release medium were studied for their impact on the release of BSA. The pulsatile releasing behavior of IPN hydrogels revealed that they can be made into microcapsules or thermo-valves, which act as an on–off release control. © 2013 Society of Chemical Industry

Cell culture and cryopreservation are necessary for clinical therapy and cells storage. The addition of 10% (v/v) foetal bovine serum (FBS) to basal culture media has been common practice and is one of the most widely used methods. FBS media added with 10% DMSO (dimethyl sulfoxide) have also been used for cryopreservation cells. Ideally, FBS should be avoided because of high cost and bio-safety. Silk sericin has been used as a serum substitute and an additive due to its good hydrophilicity and biological safety. This article summarizes a few details about the processing of sericin and its application as a serum substitute or an additive for cell culture and cryopreservation media. Sericin can be a potential novel serum substitute or an additive for cell culture and cryopreservation media.

The linearly oriented multi-walled silk fibroin/silk sericin (SF/SS) nerve conduits (NCs) can provide physical cues similar to native peripheral nerve fasciculi, but the mechanical properties of which are not excellent enough. In this study, NCs with a novel and bionic design with dual structures were developed. The important features of our NCs is that the internal skeleton (the multi-walled SF/SS conduits) has a bionic structure similar to the architecture of native peripheral nerve fasciculi, which is beneficial for nerve regeneration, and the outer sheath (the hollow poly(lactic-co-glycolic acid) [PLGA] conduits) could provide strong mechanical protection for the internal skeleton. The linearly oriented multi-walled SF/SS conduit was fabricated and inserted in the hollow PLGA sheath lumen and then used for the bridge across the sciatic nerve defect in rats. The outcome of the peripheral nerve repair post implantation was evaluated. The functional and morphological parameters were examined and showed that the novel PLGA-coated SF/SS NCs could promote peripheral nerve regeneration, approaching those elicited by nerve autografts that are the first candidate for repair of peripheral nerve defects. Thus, these updated NCs have potential usefulness to enhance functional recovery after repair of peripheral nerve defect.

WOS: 000373223000001, PubMed ID: 27032876, Background: The wound healing process is complex and still poorly understood. Sericin is a silk protein synthesized by silk worms (Bombyx mori). The objective of this study was to evaluate in vivo wound healing effects of a sericin-containing gel formulation in an incision wound model in rats. Material/Methods: Twenty-eight Wistar-Albino rats were divided into 4 groups (n=7). No intervention or treatment was applied to the Intact control group. For other groups, a dorsal skin flap (9x3 cm) was drawn and pulled up with sharp dissection. The Sham operated group received no treatment. The Placebo group received placebo gel without sericin applied to the incision area once a day from day 0 to day 9. The Sericin Group 3 received 1% sericin gel applied to the incision area once a day from day 0 to day 9. Hematoxylin and eosin stain was applied for histological analysis and Mallory-Azan staining was applied for histoimmunochemical analysis of antibodies and iNOS (inducible nitric oxide synthase), and desmin was applied to paraffin sections of skin wound specimens. Parameters of oxidative stress were measured in the wound area. Results: Epidermal thickness and vascularization were increased, and hair root degeneration, edema, cellular infiltration, collagen discoloration, and necrosis were decreased in Sericin group in comparison to the Placebo group and the Sham operated group. Malonyldialdehyde (MDA) levels were decreased, but superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx) activities were increased in the sericin group. Conclusions: We found that sericin had significant positive effects on wound healing and antioxidant activity. Sericin-based formulations can improve healing of incision wounds.

In the present study, novel adsorbents having high adsorption capability and reusability were prepared using agricultural by-products: silk sericin and lignin. Silk sericin and lignin blend beads were successfully prepared using simple coagulation methods for the removal of hexavalent chromium (Cr(VI)) from aqueous solution. A 1 M lithium chloride (LiCl)/dimethyl sulfoxide (DMSO) solvent system successfully dissolved both sericin and lignin and had sufficient viscosity for bead preparation. Compared to the conventional sericin bead adsorbent, sericin/lignin blend beads showed higher Cr(VI) adsorption capacity. The amount of lignin added to the adsorbent greatly affected the adsorption capacity of the beads, and a 50:50 sericin/lignin blend ratio was optimal. Adsorption behavior followed the Freundlich isotherm, which means the adsorption of Cr(VI) occurred on the heterogeneous surface. Cr(VI) adsorption capability increased with temperature because of thermodynamic-kinetic effects. In addition, over 90% of Cr(VI) ions were recovered from the Cr(VI) adsorbed sericin/lignin beads in a 1 M NaOH solution. The adsorption-desorption recycling process was stable for more than seven cycles, and the recycling efficiency was 82%. It is expected that the sericin/lignin beads could be successfully applied in wastewater remediation especially for hazardous Cr(VI) ions in industrial wastewater.

Semi-interpenetrating (semi-IPNs) hydrogels containing biocompatible silk sericin (SS) and poly(N-isopropylacrylamide)(PNIPAM) were prepared as novel cellular matrices. Their maximum swelling degree and basic characteristics for biomedical applications such as mouse fibroblasts (L929) cell proliferation and desorption were investigated. The results showed that the incorporation of high hydrophilic SS into PNIPAM hydrogel increased the maximum swelling degree of the semi-IPNs hydrogels, and the adhesion and growth of the L929 on semi-IPNs hydrogels were at least comparable to, or even better than, that on conventional PNIPAM hydrogel. In addition, L929 cells were found to detach from the hydrogels surface naturally by controlling environmental temperature. These results suggest great potential of semi-IPNs hydrogels in tissue engineering.

In this study, we fixed silk sericin in fabrics as a finishing product. First of all, we have extracted sericin from silkworm cocoons in order to obtain the optimum yield of sericin that is not denatured. For this reason, we have searched the optimum parameters for a favorite sericin extraction. Then, the sericin extracted was fixed onto wool and cotton fabrics in an aim to modify some of their properties. The tests of treated fabrics showed that sericin has an affinity for wool, whereas it does not have it for cotton. This affinity for wool fiber was obtained in defined conditions with about 48% exhaustion rate for a sericin concentration of 2.5% (w/w). Compared to different sericin concentrations (0%, 2.5%, 5%, 10% and 20%), a 5% of sericin (w/w) improved the wool samples touch until a score of 4 points, as well as the water’s absorption with a profit of 70.75%. The samples also showed an improved antibacterial activity.

Green synthesis of silver nanoparticles (AgNPs) using the silk sericin (SS) solution by in situ reduction at room temperature is reported. The effect of pH on the reduction reaction is studied by UV-Vis spectroscopy. The structure of the sericin-based silver nanoparticles is characterized by TEM. According to the TEM images, the average size of the silver nanoparticles is about 16 nm. The silver nanoparticles are highly dispersed and stable in silk sericin solution for monthes.

Sericin undergoes gelation by the structural transition from random coil to b-sheet transition. In the present study, the gelation time of sericin solution was investigated in the presence of NaCl, KCl and CaCl2. The addition of salts delayed the gelation time, and CaCl2 had the most pronounced effect, which delayed about 8 h at maximum. The gelation time increased with the concentration of salt. The transition of secondary structure of sericin was retarded in the presence of salt. The effect of salts on the gelation time of sericin might be due to the solvation effect of relevant cation

Sericin is a highly hydrophilic protein family acting as the glue in Bombyx mori silk. In order to apply sericin as a wound dressing, a novel sericin film named gel film was prepared by a simple process without using any chemical modifications: sericin solution was gelled with ethanol into a sheet shape and then dried. Infrared analysis revealed that the sericin gel film contained water-stable beta-sheet networks formed in the gelation step. This structural feature rendered the gel film morphologically stable against swelling and gave it good handling properties in the wet state. The sericin gel film rapidly absorbed water, equilibrating at a water content of about 80%, and exhibited elastic deformation up to a strain of about 25% in the wet state. A culture of mouse fibroblasts on the gel film indicated that it had low cell adhesion properties and no cytotoxicity. These characteristics of sericin gel film suggest its potential as a wound dressing.

Bombyx mori Sericin films were prepared with PEG-DE as cross linking agent. The main physical properties, structure characteristics, cytotoxicity and cell proliferation of sericin films were measured and analyzed. The result showed that sericin films prepared by cast method containing 30-40% of PEG-DE, showed good mechanical properties. PEG-DE caused the changes of the condensed structure of sericin films. The films prepared from sericin extracted both from silk-gland and cocoon shell showed good cytocompatibility. Silk sericin films with PEG-DE had no obvious cytotoxicity to cells.

Transglutaminases have the ability to incorporate primary amines and to graft peptides (containing glutamine or lysine residues) into proteins. These properties enable transglutaminases to be used in the grafting of a range of compounds including peptides and/or proteins onto wool fibres, altering their functionality. In this paper we investigated the transglutaminase mediated grafting of silk proteins into wool and its effect on wool properties. A commercial hydrolysed silk preparation was compared with silk sericin. The silk sericin protein was labelled with a fluorescent probe which was used to demonstrate the efficiency of the TGase grafting of such proteins into wool fibres. The TGase mediated grafting of these proteins led to a significant effect on the properties of wool yarn and fabric, resulting in increased bursting strength, as well as reduced levels of felting shrinkage and improved fabric softness. Also observed was an accumulation of deposits on the surface of the treated wool fibres when monitored by SEM and alterations in the thermal behaviour of the modified fibres, in particular for mTGase/sericin treated fibres which, with the confocal studies, corroborate the physical changes observed on the treated wool fabric.

The capability of Agaricus bisporus tyrosinase to catalyze the oxidation of tyrosine residues of silk sericin was studied under homogeneous reaction conditions, by using sericin peptides purified from industrial wastewater as the substrate. Tyrosinase was able to oxidize about 57% of sericin-bound tyrosine residues. The reaction rate was higher than with silk fibroin, but lower than with other silk-derived model peptides, i.e. tryptic and chymotryptic soluble peptide fractions of silk fibroin, suggesting that the size and the molecular conformation of the substrate influenced the kinetics of the reaction. The concentration of tyrosine in oxidized sericin samples decreased gradually with increasing the enzyme-to-substrate ratio. The average molecular weight of sericin peptides significantly increased by oxidation, indicating that cross-linking occurred via self-condensation of o-quinones and/or coupling with the free amine groups of lysine and, probably, with sulfhydryl groups of cysteine. The high temperature shift of the main thermal transitions observed in the differential scanning calorimetry curves confirmed the formation of peptide species with higher molecular weight and higher thermal stability. Fourier transform-infrared spectra of oxidized sericin samples showed slight changes related to the loss of tyrosine and formation of oxidation products. Oxidized sericin peptides were able to undergo non-enzymatic coupling with chitosan. Infrared spectra provided clear evidence of the formation of sericin–chitosan bioconjugates under homogeneous reaction conditions. Spectral changes in the NH stretching region seem to support the formation of bioconjugates via the Michael addition mechanism.

Silk sericin (SS) can be obtained as a byproduct during the silk fiber process, but its application has been limited due to the brittleness of the SS film. To enhance the flexibility of the SS film, glycerol (Glc) has been added as a plasticizer. The addition of Glc enhanced the elongation property of the SS film when the Glc content was 50-70 wt% of SS. Glc also induced the structural transition of SS from a random coil structure to a β-sheet structure. The inconsistent increase of elongation and β-sheet structure of the SS/Glc film were explained by the content of moisture in the SS/Glc film. The moisture content of the SS/Glc film increased proportionally when the Glc content was higher than 50 wt% of SS, which was the same Glc content range that exhibited the plasticizing effect. Therefore, the plasticizing effect on the SS film may occur not only because of Glc but also because of water. Furthermore, water also contributed to the increase in the β-sheet structure development. Our results suggest that the moisture content in the plasticized protein film may play an important role when the plasticizer has hygroscopic properties.

Bombyx mori silk is composed of 60-80% fibroin, 15-35% sericin and 1-5% non-sericin component including wax, pigments, sugars and other impurities. For two decades, the protein-based silk fibroin was extensively used in the research and development of medical biomaterials and biomedicines. Sericin is frequently ignored and abandoned as a byproduct or waste in the processing of traditional silk fabrics, silk floss or modern silk biomaterials. However, similar to fibroin, sericin is not only a highly useful biological material, but also a lot of biological activity. Moreover, the non-sericin component present with sericin in the cocoon shell also has a strong biological activity. In this review, the extraction and recovery methods of sericin and the non-sericin component from the cocoon layer are reported, and their composition, properties and biological activity are described to produce a comprehensive report on biomedical materials and biological drugs. In addition, related problems or concerns present in the research and development of sericin are discussed, and a potential application of sericin in sustainable development is also presented.

SynopsisObjective To investigate the effects of topical application of a Gold Silk Sericin (GSS) complex on biophysical parameters related to skin ageing. Methods A range of non-invasive bioengineering methods were deployed in an 8-week randomized, double-blinded, vehicle-controlled, split-face study among 40 female subjects aged 40–70. Endpoints measured included expert grades of skin condition, stratum corneum (SC) hydration, SC barrier function, elasticity and surface topography. Results The GSS complex produced significant single-variable (P

Sericin is an inexpensive glycoprotein obtained as a by-product in the silk industry. Its variable amino acid composition and diverse functional groups confer upon it attractive bioactive properties, which are particularly interesting for biomedical applications. Because of its antioxidant character, moisturizing ability, and mitogenic effect on mammalian cells, sericin is useful in cell culture and tissue engineering. Its positive effects on keratinocytes and fibroblasts have led to the development of sericin-based biomaterials for skin tissue repair, mainly as wound dressings. Additionally, sericin can be used for bone tissue engineering owing to its ability to induce nucleation of bone-like hydroxyapatite. Stable silk sericin biomaterials, such as films, sponges, and hydrogels, are prepared by cross-linking, ethanol precipitation, or blending with other polymers. Sericin may also be employed for drug delivery because its chemical reactivity and pH-responsiveness facilitate the fabrication of nano- and microparticles, hydrogels, and conjugated molecules, improving the bioactivity of drugs. Here, we summarized the recent advancements in the study of silk sericin for application in tissue engineering and drug delivery.

Sericin films have attracted much attention from researchers in biomedical and cosmetic fields because of its unique properties, including good cytocompatibility and its promotion of wound healing. However, poor mechanical properties of sericin films have restricted its application in these fields. In this study, a new solvent, formic acid, was used to fabricate sericin solutions and films. The effects of formic acid on the structural characteristics and mechanical properties of the sericin solutions and films were examined and compared with water. The sericin/formic acid solution showed fewer aggregated sericin molecules, resulting in a lower turbidity than that of the sericin/water solution. In addition, the gelation of the sericin solution was retarded in formic acid compared to that of water. Sericin films cast from the formic acid solution exhibited a much higher crystallinity index than that produced from water. The tensile strength and elongation of the sericin films cast from the formic acid solution were more than double that of the sericin films cast from water. It is expected that the more stable sericin solution and high-crystallinity sericin films, which have significantly improved mechanical properties, produced by using formic acid as the solvent could be utilized in biomedical and cosmetic applications.

Cell cultures often require the addition of animal serum and other supplements. In this study, silk sericin, a bioactive protein, recovered from the waste of silk floss production was hydrolysed into three pepsin-degraded sericin peptides with different ranges of molecular mass. Normal animal cells, tumour cells and hybridoma cells were cultured systematically in FBS culture media containing sericin as a supplement or serum substitute. The culture test and microscopic observation of L929 cells showed that the smaller molecular weight of the degraded sericin is most suitable for cell culture. The cell culture results showed that with the degradation of sericin, for normal mouse fibroblast L929 cells, addition of 0.75 % sericin into FBS culture medium yields cell viability that is superior to FBS culture medium alone. When all serum was replaced by sericin, cell viability in the sericin medium could reach about one half of that in FBS medium. When in a medium containing a mixture of FBS: sericin (6:4, v/v), the cell culture effect is about 80 %. For the cultures of four tumour and one hybridoma cells, regardless of the molecular weight range, these degraded sericin peptides could substitute all serum in FBS media. The cell viability and proliferation of these tumour and hybridoma cells are equivalent or superior to that in FBS medium. In other words, cell viability and proliferation of these tumour and hybridoma cells in sericin media are more preferable to serum media. The mechanism of the sericin protein to promote cell growth and proliferation will be further investigated later.

Silk sericin is the gum-like protein surrounding the fibroin in silk fibers, and generally it is removed during the fiber processing to produce fabrics. Like other silk proteins, the silk of tasar silkworms is also composed of sericin and fibroin. In this study tasar silk sericin was extracted and was confirmed to be a 70 KDa protein by SDS PAGE. The use of sericin in the field of biomedical applications has increased their use for various purposes, the extracted silk sericin was pegylated with activated PEG (MW 5000) and the conjugated product was characterized by FT-IR, 1H NMR, CD, DSC, XRD, and AF TEM and self-assembled nanoparticles were prepared.

The thermal and structural analysis of silk fibroin (SF) and silk sericin (SS) blend films reveals that the crystallization of SF is retarded in the presence of SS. Although a phase separation was observed, there might be a strong interaction at the boundary of the SF and SS through intermolecular hydrogen bonding, which restricts the conformational transition of SF.

—Silk sericin extracted from a cocoon was sulfated by chlorosulfonic acid. Sulfation of sericin was confirmed by FT-IR and the reaction efficiency was calculated as 44.9%. 1H-NMR suggested that sulfation mainly occurred at serine residues in the sericin molecule. The sulfated sericin was separated in three fractions by gel-filtration chromatography using Sephacryl S-200. The sulfate group content and amino-acid composition of each fraction were almost identical, while the anticoagulant activity differed for each fraction of sulfated sericin. Higher anticoagulant activity was observed for the higher-molecular-mass fraction. The anticoagulant activity of sulfated sericin was estimated at 1/10 to 1/20 of heparin.