Physicochemical and Functional Properties of Type B Gelatin Obtained from Nile Tilapia (Oreochromis niloticus) Scales Using Hydro-Extraction: Effect of Ultrasound Pretreatment

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Authors: Kelly Triana-Jiménez, Carlos Alonso, Milena Vega, Pablo Juanes‐Velasco, Iván Menéses-Rivera, Mario Enrique Velásquez-Lozano
Cited by: 1
References: 72

Abstract

Background: In this study, type B gelatin was extracted from Oreochromis niloticus scales under hydrothermal conditions at 60 °C to evaluate the effect of ultrasound-assisted pretreatment on its structural, physicochemical, thermal, and functional properties. Methods: Gelatin obtained with and without ultrasound pretreatment was systematically characterized through molecular weight analysis, proteomic profiling, size determination, surface morphology, proximate composition, thermal behavior, and gelation-related functional properties in order to assess the influence of the extraction method on gelation performance. Results: Ultrasound pretreatment slightly increased gelatin yield from 1.46 to 1.70%, indicating enhanced collagen solubilization. Proteomic analysis confirmed the predominance of fibrillar collagen proteins in both samples, although differences in protein distribution were observed. Furthermore, weight-average molecular weight analysis revealed a reduction from 212.3 ± 11.8 to 170.9 ± 13.2 kDa in the ultrasound-treated sample, suggesting partial fragmentation of collagen chains induced by cavitation effects. Structural modifications were also reflected in increased porosity and surface changes, contributing to improved colloidal stability. However, these changes significantly affect the functional behavior of the gelatin. Ultrasound-treated sample exhibited limited gel-forming capacity and failed to form stable gels at the evaluated concentration, despite complete dissolution. In contrast, gelatin extracted without ultrasound treatment retained higher-molecular-weight fractions and formed stable gels at both 5 and 10% (w/w). Thermal and spectroscopic analyses suggested that the fundamental collagen structure was preserved in both samples, although differences were observed in thermal degradation behavior. Conclusions: These results highlight the importance of controlling ultrasound-assisted extraction conditions to balance collagen recovery with the preservation of molecular integrity required for gelation, providing insights for the development of sustainable fish-derived biomaterials for pharmaceuticals and biomedical applications.

Fields of Study & Subjects

Collagen: Extraction and Characterization Nanocomposite Films for Food Packaging Protein Hydrolysis and Bioactive Peptides

Publication details

Journal / source
Pharmaceutics
Publisher
MDPI AG
Volume
18
Issue
4
Pages
463–463
Publication date
9 April 2026
Language
EN