Extraction of Collagen/Gelatin from the Marine Demosponge Chondrosia reniformis (Nardo, 1847) Using Water Acidified with Carbon Dioxide – Process Optimization

Abstract

Marine sponges are a rich source of natural bioactive compounds. One of the most abundant valuable products is collagen/ gelatin, which presents an interesting alternative source for pharmaceutical and biomedical applications. We have previously proposed an innovative green technology for the extraction of collagen/gelatin from marine sponges based in water acidified with carbon dioxide. In this work, we have optimized the process operating conditions toward high yields and collagen quality as well as to reduce extraction procedure duration and energy consumption. The process extraction efficiency is higher than 50%, corresponding to a yield of approximately 10% of the sponge dry mass, obtained for mild operating conditions of 10 bar and 3 h. The extracted material was characterized by scanning electron microscopy (SEM), rheology, Fourier transformed infrared spectroscopy (FTIR), circular dichroism (CD), amino acid analysis, and SDS-PAGE. The extracts were found to be composed of highly pure mixtures of collagen and gelatin with similar properties to collagen isolated from other marine sources. The cytotoxicity evaluation, performed with L929 cells, has proven the biocompatibility of the material extracted. Overall, the results obtained demonstrate the efficiency of this approach and the high industrial potential of this technology to obtain marine collagen/gelatin with properties suitable for biomedical applications.

Acid and enzymatic extraction of collagen from Atlantic cod (Gadus Morhua) swim bladders envisaging health-related applications

“…The spectra shown very similar profiles, suggesting that the extracts present similar structures and chemical compositions, with the characteristic peaks of Amide A, Amide B, Amide I, Amide II and Amide III being clearly visible. These findings are similar with other found in literature for other marine species [12,22,[26][27][28], as well as with collagens extracted from cod skin, also displayed in Figure 2 as reference. The N-H stretching vibration typical of intermolecular hydrogen bonding, commonly observed in a range between 3000-3500 cm À1 , is relative to the Amide A band and was here observed at 3400 cm À1 .…”

“…ASCsb and PSCsb presented a flow behavior index g ¼ 0.33 ± 0.01 and g ¼ 0.61 ± 0.16, respectively, characteristic of non-Newtonian fluids (for Newtonian liquid, n ¼ 1, pseudo plastic fluid n < 1 and swelling plastic fluid n > 1). Moreover, ASCsb and PSCsb samples exhibits a typical shear thinning behavior for different shear rates, characterized by a decrease in the viscosity with increasing shear rate and a linear relationship between the shear rate and shear stress [26]. This shear-thinning (pseudo plastic) behavior, also present in hyaluronic acid aqueous solutions [43,44], reveals to be an interesting rheological property regarding its further processing, namely on the production of different types of biomaterials, including injectable systems, envisaging biomedical application, namely on tissue engineering and regeneration, but also as component in cosmetic formulations.…”

Cosmetic Potential of Marine Fish Skin Collagen

“…Other sources such as marine collagen are arising as a relevant alternative to their mammalian counterparts. Several organisms such as marine sponges [5,6], jellyfish [7,8], squid [9,10], and fishes [11][12][13][14] have been exploited for the extraction of marine collagen. About 75% of a fish's…”

Collagen from Marine Biological Sources and Medical Applications

“…glycine levels in collagen from marine sponge ( Chondrosia reniformis ) was found to be 18.9% and hydroxyproline 40% in the study done by Swatschek et al . The same species was recently found to have 31.6% glycine and 47.3% hydroxyproline content . This discrepancy can be explained by the fact that in addition to collagen, marine tissues contain other proteins such as glycoproteins which are known to be strongly associated with collagen and appear as impurities thus affect the purity of the extracted collagen.…”