Sericin Protein: Structure, Properties, and Applications

被引:5
作者
Aad, Rony [1 ]
Dragojlov, Ivana [1 ]
Vesentini, Simone [1 ]
机构
[1] Politecn Milan, Dept Elect Informat & Bioengn, I-20133 Milan, Italy
关键词
sericin; silk; biobased materials; extraction processes; silkworm <italic>Bombyx mori</italic>; IN-VITRO MATURATION; SILK-SERICIN; BOMBYX-MORI; ALKALINE PROTEASE; CITRIC-ACID; AMINO-ACIDS; EXTRACTION; NANOPARTICLES; FABRICATION; HYDROGEL;
D O I
10.3390/jfb15110322
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
Silk sericin, the glue protein binding fibroin fibers together, is present in the Bombyx mori silkworms' cocoons. In recent years, sericin has gained attention for its wide range of properties and possible opportunities for various applications, as evidenced by the meta-analysis conducted in this review. Sericin extraction methods have evolved over the years to become more efficient and environmentally friendly, preserving its structure. Due to its biocompatibility, biodegradability, anti-inflammatory, antibacterial, antioxidant, UV-protective, anti-tyrosinase, anti-aging, and anti-cancer properties, sericin is increasingly used in biomedical fields like drug delivery, tissue engineering, and serum-free cell culture media. Beyond healthcare, sericin shows promise in industries such as textiles, cosmetics, and food packaging. This review aims to highlight recent advancements in sericin extraction, research, and applications, while also summarizing key findings from earlier studies.
引用
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页数:36
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