Marine Collagen and its Biotechnological Applications

Pozzolini, Marina; Scarfı̀, Sonia; Giovine, Marco

doi:10.1002/9781119143802.ch39

Cited by 4 publications

(2 citation statements)

References 142 publications

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“…The alkaline environment aids in the hydrolysis of fish collagen, the primary source of protein for gelatin production. This hydrolysis process breaks down collagen into smaller peptides and amino acids, facilitating the subsequent extraction of gelatin (Pozzolini et al, 2020). 2.…”

Section: Results and Discussion Extraction Of Fish-based Gelatinmentioning

confidence: 99%

Fish-based gelatin: exploring a sustainable and halal alternative

Reza,

Annissa

2023

J. Halal Sci. Res.

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Gelatin derived from fish has emerged as a promising alternative to traditional gelatin derived from mammals, primarily due to its potential to meet the rising demand for halal-certified products. This article provides a comprehensive overview of the utilization and extraction of gelatin derived from fish as a halal-compliant substitute. This study gathered information regarding the source, extraction method, and contribution to physicochemical properties and applications by reviewing the relevant literature. It discusses the most frequently consumed fish species, such as tilapia, mackerel, and catfish, which are halal and possess outstanding gel-forming properties. Type A gelatine (pre-treated acid) is distinguished from type B gelatine (pre-treated alkaline) based on the solvent used for pre-treatment. Seventy-five percent of the twenty gelatin extraction studies utilized alkaline pre-treatment (i.e., NaOH), where the base solution can eliminate non-collagen from the skin or bone of fish, thereby obtaining pure collagen. All extraction processes are conducted using the hot water extraction method at temperatures ranging from 45 to 70 °C. This method is time-efficient, accelerates collagen decomposition and gelatin solubility, and increases gelatin yield (from 5.33 to 68.75%). The effects of various procedures, including acid and alkaline extraction, on gelatin gel strength, moisture content, ash content, protein content, and fat content are investigated. According to SNI, gelatine has a gel strength between 50 and 300, a moisture content that does not exceed 16%, a lipid content that does not exceed 5%, and an average protein content that does not exceed 87.65%. However, ash concentrations typically persist above 3.25%, presumably due to using bases in pre-treatment processes that do not perfectly dissolve minerals compared to acids. In conclusion, the source and method of extraction will impact the gelatin's characteristics and applications. Keywords: Gelatin, Fish-based gelatin, Physicochemical properties, Traditional gelatin, SNI

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Section: Results and Discussion Extraction Of Fish-based Gelatinmentioning

confidence: 99%

Fish-based gelatin: exploring a sustainable and halal alternative

Reza,

Annissa

2023

J. Halal Sci. Res.

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“…Basic knowledge of sponge collagen‐based morphology and morphogenesis of biomaterials (Garrone, 1998 ) is fundamental in research focusing on sponges as producers of structurally and mechanically interesting biomaterials, such as diversified and abundant collagenic structures (Da Hora et al, 2018 ; Eherlich et al, 2018 ; Exposito et al, 1990 , 1991 , 2002 ; Heinemann et al, 2007 ; Langasco et al, 2017 ; Lim et al, 2019 ; Martins et al, 2019 ; Nicklas et al, 2009a , 2009b ; Pallela et al, 2012 ; Pozzolini et al, 2012 , 2020 ; Schröder et al, 2000 ; Silva et al, 2014 ; Tziveleka et al, 2017 ; Wang et al, 2010 ). Key points for marine bioinspired technological research are: (i) correct taxonomic identification of target species to standardize processes, (ii) In depth knowledge of functional morphological traits useful for the comprehension of a potential role as biomaterials characterizing body architecture of target species, (iii) exploitation of renewable resources provided by target biomass in the context of a sustainable mariculture and conservation strategies.…”

Section: Introductionmentioning

confidence: 99%

Collagenic architecture and morphotraits in a marine basal metazoan as a model for bioinspired applied research

Manconi

Cubeddu

Pronzato

et al. 2022

Journal of Morphology

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In some Porifera (Demospongiae: Keratosa), prototypes of the connective system are almost exclusively based on collagenic networks. We studied the topographic distribution, spatial layout, microtraits, and/or morphogenesis of these collagenic structures in Ircinia retidermata (Dictyoceratida: Irciniidae). Analyses were carried out on a clonal strain from sustainable experimental mariculture by using light and scanning electron microscopy. Histology revealed new insights on the widely diversified and complex hierarchical assemblage of collagenic structures. Key evolutionary novelties in the organization of sponge connective system were found out. The aquiferous canals are shaped as corrugate‐like pipelines conferring plasticity to the water circulation system. Compact clusters of elongated cells are putatively involved in a nutrient transferring system. Knob‐ended filaments are characterized by a banding pattern and micro‐components. Ectosome and outer endosome districts are the active fibrogenetic areas, where exogenous material constitutes an axial condensation nucleus for the ensuing morphogenesis. The new data can be useful to understand not only the evolutionary novelties occurring in the target taxon but also the morpho‐functional significance of its adaptive collagenic anatomical traits. In addition, data may give insights on both marine collagen sustainable applied researches along with evolutionary and phylogenetic analyses, thus highlighting sponges as a key renewable source for inspired biomaterials. Therefore, we also promote bioresources sustainable exploitation with the aim to provide new donors of marine collagen, thereby supporting conservation of wild populations/species.

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