China
Africa
Explore chapters and articles related to this topic
Polymeric Biomaterials in Tissue Engineering
Published in Chander Prakash, Sunpreet Singh, J. Paulo Davim, Functional and Smart Materials, 2020
Akhilesh Kumar Maurya, Nidhi Mishra
Silk is a natural polymeric biomaterial that is made up of protein fiber. Silk protein fibers are mainly composed of fibroin and are synthesized by certain larvae of insect to form cocoons [25]. Mulberry silkworm, i.e., Bombyx mori and spiders of Nephila genus (N. clavipes, N. madagascarensis) provide the best-known silk by cocoons of the larvae. Fibrous silks are synthesized by the epithelial cells of these living insects [19]. Silk synthesized by the silkworm consists of two main proteins, sericin, and fibroin. Fibroin is made up of the amino acids Gly-Ser-Gly-Ala-Gly-Ala and forms β-pleated structure due to a 59-mer amino acid repeat with variation in some sequence [26]. Hydrogen bond forms between polypeptide chains, and side chains form hydrogen bond network above and below the plane [27]. Fibroin has a very interesting application in the medical field, and serisin is used to obtain polymeric biomaterials and used in tissue engineering [28]. (See Figure 2.3)
Bionanocomposites Based on Silk Proteins and Nanoclay
Published in Mangala Joshi, Nanotechnology in Textiles, 2020
For extraction of sericin, silk cocoons are cut into small piece and boiled in an autoclave at 120°C for 1 h, keeping the material-to-liquor ratio at 1:15. This process is known as a high temperature/high pressure degumming process. The sericin-extracted aqueous solution is then filtered with muslin cloth to remove fibroin and other suspended impurities. Solid sericin (above MW 250 kDa) powder is obtained by heating the sericin solution at 40°C or by freeze drying or spray drying it. Figure 6.4 shows the general procedure adopted for the formation of silk/clay nanocomposites.
Manufacturing and Assembly of Micro- and Nanoscale Devices and Interfaces Using Silk Proteins
Published in Hyun Jung Kim, Biomimetic Microengineering, 2020
Silk fibroin is kind of protein extracted from silkworm cocoon and has been successfully used in a variety of areas, such as optical sensing and implantable medical device. In fact, silk cocoon mainly contains two types of proteins: silk fibroin and sericin. Sericin also shows valuable bioactivities, such as cell adhesion, low immunogenicity, biocompatibility, and biodegradability, which makes it widely utilized in drug delivery, regenerative medicine and tissue engineering.
Highly selective and sensitive colorimetric detection of arsenic(III) in aqueous solution using green synthesized unmodified gold nanoparticles
Published in Journal of Dispersion Science and Technology, 2023
K. S. Harisha, B. Narayana, Y. Sangappa
Silk is the only source of sericin and can be extracted using different methods include urea-extracted, acid degraded, alkali degraded and heat degraded sericin.[34] In our case, heat degraded method or degumming procedure was used. In a brief, fresh silk cocoons (2 g) of B. mori CB gold were made small pieces and boiled in double distilled water (DDW, 250 mL) for ∼50 min. Afterward, the resulted solution was cooled at room temperature and fibroin mass squeezed and removed. Then, the obtained sericin solution was filtered using a Whatman paper No. 1 and was centrifuged at 4000 rpm for ∼30 min to eliminate unwanted silk fibroin mass persisted in the process. The pure SS is well-maintained by keeping at 4 °C for further experiment. Further, the degumming weight loss of the samples was determined using the relation,[35] where M1 is the initial mass of silk cocoons, M2 is the loss mass of degummed silk fibroin. In the current work, 2 g of cocoons were used for degumming, and the pure fibroin mass arrived in the experiment was 1.27 g. Therefore, the weight loss is 36.5%. Using this we have calculated the sericin weight % (yield) and can be expressed as weight loss of silk fibroin in desired volume.[36] Hence, weight % of sericin is,
Proliferation of mouse embryonic stem cells on substrate coated with intact silkworm sericin
Published in The Journal of The Textile Institute, 2022
Chihiro Umehara, Ai Ai Lian, Yuichiro Funahashi, Keiko Takaki, Rina Maruta, Yuto Ohmaru, Yoko Okahisa, Takashi Aoki, Hajime Mori, Eiji Kotani
During silk processing, sericin is typically degraded and discarded as waste. In recent decades, sericin, which exhibits biologically important activities, such as low immunostimulation in mammals, has shown potential as a useful biomedical material (Kunz et al., 2016). The conjugation of sericin to the clinically important peptide insulin or proteins such as L-asparaginase has been found to stabilize and prolong its bioactivity in vivo and in vitro (Zhang et al., 2006a; 2006b). Additionally, sericin potentially contributes to tissue engineering as a substitute for supplements in cell culture systems or processed materials for scaffolds (Arango et al., 2021; Joseph & Raj, 2012; Kunz et al., 2016; Terada et al., 2002). In addition, sericin has specific properties in dermatological and cosmetic use to inhibit the activities of enzymes, such as tyrosinase (Kato et al., 1998), elastase (Chlapanidas et al., 2013), and oxidase (Kato et al., 1998). This evidence demonstrates the efficacy of sericin in physiological regulation in biological systems.
Sericin from mulberry and non-mulberry silk using chemical-free degumming
Published in The Journal of The Textile Institute, 2022
Monalisa Kalita, Benjamin J. Allardyce, Kamatchi Sankaranarayanan, Dipali Devi, Rangam Rajkhowa
Silkworm silk filament consists of two proteins: fibroin, the main structural protein forming the fiber and sericin, the glue-like coating that helps to bind the filament and form the cocoon. Apart from textiles, silk fibroin is preferred for non-textile applications due to its biocompatibility, biodegradability and good mechanical properties (Bhardwaj & Kundu, 2011; Das et al., 2013; Yan et al., 2012). In the textile industry the removal of sericin is important to improve the smoothness and luster of the fiber, and facilitate dye penetration. However, interest in sericin coming as waste from industry has emerged in recent years as a useful biopolymer because of several desirable properties such as excellent moisture retention, controllable gelation, and UV resistance. Sericin has been investigated for applications such as cosmetics (Chlapanidas et al., 2013; Kato et al., 1998; Sheikh et al., 2015), wound healing (Lamboni et al., 2016) and as an additive for cell culture media (Bari et al., 2018; Sahu et al., 2016; Terada, 2007). A well characterized sericin has potential applications as a useful protein in biomedical, cosmetic, food and industrial applications due to its biocompatibility, moisture sorption, and gelling properties.