Banca de DEFESA: VANESSA RICAS BIANCARDI

Uma banca de DEFESA de DOUTORADO foi cadastrada pelo programa.
STUDENT : VANESSA RICAS BIANCARDI
DATE: 21/10/2024
TIME: 14:00
LOCAL: Letis - IT UFRRJ
TITLE:

Bovine bone technologies for obtaining type I collagen - Analysis of processing, demineralization, enzymatic hydrolysis and gel formation processes for use in food

KEY WORDS:

collagen, bone waste, bone tissue, sustainability, circular economy, innovation, food industry.

PAGES: 92
BIG AREA: Ciências Agrárias
AREA: Ciência e Tecnologia de Alimentos
SUBÁREA: Tecnologia de Alimentos
SUMMARY:

The functionalities of collagen were driven by the growing interest in agro-industrial production waste. Collagen is the predominant protein in the fibrous tissues of animals, such as bones. Bone is predominantly composed of type I collagen fibers sequenced together with mineral crystals. Type I collagen is a biopolymeric protein with a fibrous structure, featuring a characteristic triple helix that provides properties of self-assembly and biocompatibility. Type I collagen retains the same properties when isolated from the source material. Obtaining Type I collagen from bovine bone was not feasible due to its natural rigidity until recent studies presented alternatives to overcome this limitation and enable its processing. This thesis aimed to elucidate technologies using bone waste through the necessary methodologies for the reuse of bovine bone and to enable the extraction of type I collagen by transforming the by-product for use in food. Four scientific studies were conducted and presented in chapters I, II, III, and IV. Chapter I summarized and evaluated the current literature on studies that investigated the extraction of collagen and gelatin from bone waste, reviewed studies that used bone collagen as a binding agent, and summarized studies that used collagen and gelatin from agro-industrial waste in food. Advances have been made in the extraction of collagen and gelatin from bone, and there are technological and sustainable prospects for promising applications in food. The information presented aimed to provide new extraction strategies, research advancements, and applications of sustainable practices. Chapter II investigated the physicochemical properties of the bovine tibia bone matrix after processing and demineralization. The bone matrix was solubilized in acetic acid followed by lactic acid. The bone matrix was analyzed for percentages of ossein and hydroxyapatite by nitrogen and ash content, mineral content, particle size distribution, Fourier-transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), and scanning electron microscopy (SEM). The pH and mineral content of the residual extracts were also analyzed. Acid solubilization affected the physicochemical properties of the osseinhydroxyapatite. The bone matrix solubilized by acetic and lactic acid showed preservation of ossein along with the loss of hydroxyapatite. The availability of type I collagen after the processes was revealed, providing a viable alternative for bovine bone demineralization. Chapter III obtained collagen gel from the bovine tibia and used it in the formation of selfassembling hydrogels with xanthan gum and transglutaminase. Collagen gel was obtained through processing, demineralization, and hydrolysis using commercial proteases. The processes were analyzed for the degree of hydrolysis, yield, protein content, and hydroxyproline content. The selected collagen gel was analyzed for solubility, differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), FTIR, and fluorescence microscopy. Selfassembling hydrogels with xanthan gum and transglutaminase were formulated with the selected collagen gel. The hydrogels were analyzed using FTIR and fluorescence microscopy. The results confirmed the biocompatibility of collagen gel with xanthan gum and transglutaminase, revealing collagen gel as a potential ingredient for protein-based products. Chapter IV extracted collagen from the bovine tibia and analyzed its composition, structural, and thermal properties through physical analyses. Collagen in gel-form was obtained through processing, demineralization, and hydrolysis using commercial protease. The collagen was analyzed using DSC, TGA, FTIR, XRD, SEM, and energy-dispersive spectroscopy (EDS). DSC and TGA showed heat stability. FTIR displayed the respective collagen peptides. XRD showed diffraction peaks. SEM-EDS revealed minimal residual mineral elements. The results were promising, revealing collagen with desirable properties for protein-based products. In conclusion, by promoting the reuse of bone waste and validating technologies from the bovine tibia, this thesis enhances the accessibility of the involved methodologies, significantly contributing to the reduction of agro-industrial waste and promoting sustainability. The research reinforces the circular economy by offering biotechnological solutions that add value to waste materials.

COMMITTEE MEMBERS:
Interno - 2455049 - JOSE LUCENA BARBOSA JUNIOR
Externa ao Programa - 1898760 - RENATA NUNES OLIVEIRA - UFRRJExterno à Instituição - MARCO ANTONIO TRINDADE - USP
Externa à Instituição - ALESSANDRA LOPES DE OLIVEIRA - USP
Externo à Instituição - MARIA GABRIELA BELLO KOBLITZ - UNIRIO