Biotechnological valorization of marine collagens: biomaterials for health applications

This chapter focuses on the fibril forming collagens type I, II, III; collagen type V and the basement membrane collagen type IV, given either their abundance, relevance to regeneration processes and possibility to purify those collagens from marine organisms. Fishes are certainly the most investigated source for the extraction of collagen, gelatine and collagenous peptides. Collagen and derived products can be extracted from skin, scales, bones and cartilages. The chapter provides an overview, as complete as possible, of the collagens successfully extracted from marine organisms. Collagen extraction and purification methods, as well as the final yield, mostly depend on the species used as a source, the starting material (i.e. anatomical part) and also the age of the specimens. It is possible to roughly separate collagens into four different categories: acid soluble collagen, pepsin soluble collagen, salt soluble collagen and insoluble collagen

Modifying fish gelatin electrospun membranes for biomedical applications: cross-linking and swelling behavior

Development of suitable membranes is a fundamental requisite for tissue and biomedical engineering applications. This work presents fish gelatin random and aligned electrospun membranes cross-linked with glutaraldehyde (GA). It was observed that the fiber average diameter and the morphology is not influenced by the GA exposure time and presents fibers with an average diameter around 250 nm. Moreover, when the gelatin mats are immersed in a phosphate buffered saline solution (PBS), they can retain as much as 12 times its initial weight of solution almost instantaneously, but the material microstructure of the fiber mats changes from the characteristic fibrous to an almost spherical porous structure. Cross-linked gelatin electrospun fiber mats and films showed a water vapor permeability of 1.37 ± 0.02 and 0.13 ± 0.10 (g.mm)/(m2.h.kPa), respectively. Finally, the processing technique and cross-linking process does not inhibit MC-3T3-E1 cell adhesion. Preliminary cell culture results showed good cell adhesion and proliferation in the cross-linked random and aligned gelatin fiber mats.This work is funded by FEDER funds through the "Programa Operacional Factores de Competitividade - COMPETE" and by the national funds arranged by FCT-Fundacao para a Ciencia e a Tecnologia, project references NANO/NMed-SD/0156/2007, PTDC/CTM-NAN/112574/2009, and PEST-C/FIS/UI607/2011. The authors also thank funding from Matepro - Optimizing Materials and Processes," ref. NORTE-07-0124-FEDER-000037," co-funded by the "Programa Operacional Regional do Norte" (ON.2 - O Novo Norte), under the "Quadro de Referencia Estrategico Nacional" (QREN), through the "Fundo Europeu de Desenvolvimento Regional" (FEDER). The authors also thank support from the COST Action MP1003, 2010 "European Scientific Network for Artificial Muscles." V. Sencadas, J. Padrao, and J. Silva thank the FCT for the SFRH/BPD/64958/2009, SFRH/BD/64901/2009, and SFRH/BPD/63148/2009 grants, respectively