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Anti-inflammatory Potential of Chitin, Chitosan and Chitooligosaccharides: A Review
( Gaurav Lodhi ),( Yon Suk Kim ),( Jin Woo Hwang ),( Se Kwon Kim ),( You Jin Jeon ),( Sang Ho Moon ),( Byong Tae Jeon ),( Pyo Jam Park ) 한국키틴키토산학회 2014 한국키틴키토산학회지 Vol.19 No.3
Inflammation is primarily a defense mechanism of the host against invading pathogens with the main purpose being mainte-nance of tissue homeostasis. However, if it goes uncontrolled or unchecked, it leads to a plethora of pathological conditions including tissue damage, tumorogenesis and even organ failure. Chitin is a non-toxic, natural biopolymer synthesized in enor-mous amount by living organism. Chitosan is a partially deacetylated derivative of chitin. Both chitin and chitosan have been in the center of research because of their functional properties but poor solubility limits their application. Chitooligosaccharides(COS) are chemically or enzymatically degraded products of chitosan or chitin with an advantage of increased solubility. The application of chitin, chitosan and COS varies from being used in food, cosmetics, biomedicine, agriculture, environmental protection, and waste water management to being used as a bioactive material and carriers in drug delivery. In light of the various proven biomedical applications of chitin, chitosan and COS, this review focuses on their anti-inflammatory potential.
Isolation and characterisation of collagen from elk antler velvet
Lee, Do Hun,Hong, Heeok,Lodhi, Gaurav,Cheong, Sun Hee,Park, Pyo Jam,Hu, Tiejun,Sangwoo, Kim,Moon, Sang Ho,Jeon, Byong Tae CSIRO Publishing 2014 Animal Production Science Vol.54 No.8
<P> Collagen was extracted from the antler velvet of elk (Cervus elaphus). Two types of collagen were prepared namely, acetic acid-soluble collagen and pepsin-soluble collagen. The electrophoretic patterns of both of the collagens showed that they were heterotrimeric, i.e. they consisted of α1α2α3. The total yield of the collagen obtained from the elk antler velvet was 12.1%. Amino acid analysis of the collagen by high-performance liquid chromatography showed that imino acid content such as that of proline and hydroxyproline was high, which might contribute to better visco-elastic properties. The peptide mapping of the collagens showed their similarity with porcine Type I collagen, thereby suggesting that the primary structure of both collagens is identical to that of porcine skin Type I collagen. The thermal denaturation temperature was 37°C, which is comparable to porcine Type I collagen and may also be as a result of high imino acid content. </P>