Isolation and partial characterization of collagen from outer skin of Sepia pharaonis (Ehrenberg, 1831) from Puducherry coast

Jayalakshmi Krishnamoorthi; Pasiyappazham Ramasamy; Vairamani Shanmugam; Annaian Shanmugam

doi:10.1016/j.bbrep.2017.02.006

Isolation and partial characterization of collagen from outer skin of Sepia pharaonis (Ehrenberg, 1831) from Puducherry coast

Biochem Biophys Rep. 2017 Feb 27:10:39-45. doi: 10.1016/j.bbrep.2017.02.006. eCollection 2017 Jul.

Authors

Jayalakshmi Krishnamoorthi^{1

2}, Pasiyappazham Ramasamy^{1

3}, Vairamani Shanmugam^{1

4}, Annaian Shanmugam¹

Affiliations

¹ CAS in Marine Biology, Faculty of Marine Sciences, Annamalai University, Parangipettai 608502, Tamil Nadu, India.
² Department of Zoology, Tagore Arts College, Puducherry 605008, India.
³ Department of Microbiology, School of Life Sciences, Pondicherry University, Puducherry 605014, India.
⁴ Government college of Education, Vellore, 632006 Tamil Nadu, India.

Abstract

Type I collagen from outer skin of Sepia pharaonis was extracted and partially characterized. Yield of Acid Soluble Collagen (ASC) and Pepsin Soluble Collagen (PSC) were calculated as 1.66% and 3.93% and the total protein content of ASC and PSC were found as 18.4% and 48.6%. FT-IR spectrum of ASC and PSC recorded 12 and 14 peaks, respectively. ¹H NMR spectrum of ASC showed singlets at 1.23 ppm, 3.1 ppm, 3.55 ppm and 3.7 ppm and PSC at 1.23 ppm and 2.08 ppm. The molecular weight for ASC was calculated as 102 kDa and for PSC as 110, 108 and 102 kDa through SDS-PAGE. Differential Scanning Calorimetry (DSC) results supported that PSC withstand high thermal stability (82.85 °C) than ASC (73.13 °C). Higher denaturation temperature with high molecular weight well support the property of type I collagen from skin of S. pharaonis and it could be used as another potent source for the extraction of collagen.

Keywords: 1H-NMR; ASC; Collagen; DSC; PSC; Sepia pharaonis.