Nutritional composition of liver (Digestive gland) from thondi squid (Sepioteuthis lessoniana)

1398-1403The present study was undertaken to investigate the nutritional composition such as protein, lipid, carbohydrate, and ash of Sepioteuthis lessoniana liver. The liver was collected from the fish landing centre and the proximate composition total protein, carbohydrate and lipid content were found to be 31.16 ± 0.28%, 3.9 ± 0.05% and 21.06 ± 0.11%, respectively. The moisture and ash content of the S. lessoniana liver were recorded as 52.1 ± 0.17 % and 8.03 ± 0.05 %, respectively. The heavy metal content was estimated by acid digestion method and was found to be as follows: Cd-0.020 ppm, Cu-2.723 ppm, Mn-1.121 ppm, Ni-0.109 ppm, Pb-0.190 ppm, and Zn - 0.522 ppm. The present study concluded that the S. lessoniana liver (non-edible part) is suitable for human consumption, and is good for aquaculture and poultry feed formulations

Extraction, structural and physical characterization of type I collagen from the outer skin of Sepiella inermis (Orbigny, 1848)

The acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were extracted from the outer skin of Sepiella inermis and further characterized partially. The yield of ASC was low (0.58% on dry weight basis); whereas the yield of PSC was comparatively more (16.23% on dry weight basis). The protein content in ASC and PSC was calculated as 20.24 and 69.56%, respectively (on dry weight basis). The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) gel profile showed two bands for ASC and PSC with corresponding molecular weight of 86 and 67 kDa and 86, 63 and 58 kDa respectively. The differential scanning calorimetry (DSC) results showed that ASC withstand up to 75.93°C whereas the PSC withstand up to 75.05°C. The fourier transform infrared spectroscopy (FT-IR) spectrum of both ASC and PSC recorded 11 and 13 peaks, respectively. The fine structure of both ASC and PSC was also studied using scanning electron microscopy (SEM).Key words: Sepiella inermis, acid soluble collagen (ASC), pepsin soluble collagen (PSC), differential scanning calorimetry (DSC), fourier transform infrared (FT-IR) spectroscopy, scanning electron microscopy (SEM)

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

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

Isolation, characterization and molecular weight determination of collagen from marine sponge Spirastrella inconstans (Dendy)

Collagen is a major structural protein of connective tissues. It can be used as a prosthetic biomaterial applicable to artificial skin, tendon ligaments and development collagen implants. In the present study, an attempt was made to isolate and characterize collagen from the marine sponge, Spirastrella inconstans. The total protein content of sponge collagen was relatively high (32%). While determining the molecular weight of crude and purified collagen through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), the crude showed three bands (80, 60 and 59 kDa molecular weight) and purified showed only a single band (58 kDa). The structural properties were analyzed by using fourier transform infra red (FT-IR) spectrum and the stability of collagen was also given the single transition peak in differential scanning calorimetry (DSC). The microstructure of sponge collagen showed highly porous and interconnected scaffolds in scanning electron microscopic (SEM) analysis.Keywords: Collagen, Spirastrella inconstans, SDS-PAGE, Fourier transform infrared (FT-IR), differential scanning calorimetry (DSC), scanning electron microscopy (SEM)African Journal of Biotechnology Vol. 12(5), pp. 504-51