Chemical structure |
Spongin is a collagen derivative protein which can be referred to halogenated scleroproteins or neurokeratin-like proteins [231,232]. However, halogens (I, Br), detected within spongin structure, do not occur in collagens or keratins [232]. The biochemistry of spongin as well as its molecular weight remains to be unknown. |
Physicochemical properties |
Spongin is not soluble neither by proteases (collagenase, pepsin, trypsin, amylase, lysozyme), nor by aggressive reagents, i.e., HCl, sulfuric acid, hydrogen peroxide [233,234,235]. Treatment with alkalis dissolves spongin resulting in hydrolysates of amino acids. In the natural habitat of sponges, spongin can be destroyed by bacteria and fungi [235]. Its thermostability is species dependent and ranges between 150 °C and 360 °C [236]. Owing to spongin, the scaffolds of bath sponge Spongia officinalis are characterized by unique material properties, such as the ability to hold water, toughness, compressibility and resiliency [232]. Heating of spongin scaffolds up to 1200 °C under exclusion of oxygen leads to obtaining of turbostratic graphite [86]. |
Spongin extraction/Physical form after extraction |
Spongin skeletons can be purified using 3M HCl as was shown for Hippospongia communis [237]. |
Biomaterials properties (biocompatibility, biodegradability, toxicity, immune responses) |
Spongin was reported to be biocompatible, biodegradable, non-toxic and of low immunogenicity [4,232,238,239]. |
Market situation (world market reports) |
According to Technavio report, global commercial sponge market is predicted to reach USD 3.18 billion during 2020–2024 [240]. In addition, sponges can be cultivated and such sponge farms already exist in Japan, France, Greece, the Philippines, Micronesia, Australia, New Zealand, and East Africa [232]. |
Patents |
Currently, about several hundreds of patents on sponge cultivation, sponge scaffolds extraction, their treatments, and applications exist. |
For search, use: https://patents.google.com/
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Selected examples: |
WO2015151030A1. Method to obtain collagen/gelatin from marine sponges |
WO2006089660A2. Method for cleaning marine collagen and the treatment thereof to form porous sponges |
US20030032601A1. Method for isolating sponge collagen and producing nanoparticulate collagen, and the use thereof |
US20080261876A1. Method for purifying marine collagen and the processing thereof into porous sponges |
US20100260823A1. Preparation with marine collagen for protease inhibition |
JPH07100B2. Method of drying collagen sponge |
DE10010113A. Native sponge collagen, process for its isolation and its use, as well as native nanoparticulate sponge collagen, process for its preparation and its use |