Banca de DEFESA: ANNA CAROLINA BATISTA E SILVA

Uma banca de DEFESA de MESTRADO foi cadastrada pelo programa.
STUDENT : ANNA CAROLINA BATISTA E SILVA
DATE: 29/05/2026
TIME: 14:00
LOCAL: Auditório da PRPG
TITLE:

Powdered preparation development containing collagenolytic proteases for potential use in veterinary medicine

KEY WORDS:

Aspergillus heteromorphus; Lyophilization; Spray-dryed; Enzymatic stability

PAGES: 104
BIG AREA: Ciências Agrárias
AREA: Medicina Veterinária
SUMMARY:

Collagenases have broad application potential in the leather, cosmetic, food, and medical fields, especially in wound healing. Microorganisms, such as filamentous fungi of the genus Aspergillus, represent advantageous sources of these enzymes due to their high productivity and extracellular secretion. To enhance the stability and shelf life of these enzymes, drying techniques (lyophilization and spray-dried) have been applied to efficiently and economically obtain powdered enzymatic preparations. This study consisted of a bibliometric analysis using the Web of Science database, with the search terms “Collagenase AND healing AND (veterinary OR animal),” conducted with the aid of VOSviewer software. The search yielded 35 scientific articles on the direct application of collagenase in animal models. The analysis showed that the field is still limited and fragmented, with restricted co-authorship networks and low international collaboration, and that applications are mainly concentrated in studies of enzymatic digestion, cell isolation, induction of tendon pathologies, as well as wound healing and enzymatic debridement. In addition, a powdered enzymatic preparation containing proteases with collagenolytic activity was developed. For this purpose, the microorganism A. heteromorphus was cultivated on wheat bran (3 g, 20% moisture) at 30 °C for 96 hours. The crude extract was subjected to precipitation with 70% acetone and purified by ion-exchange chromatography on DEAE-Sephadex A50, using 0.1 M Tris-HCl buffer (pH 8.0). The liquid, lyophilized powder, and spray-dried formulations were stored under refrigeration, and their proteolytic activity was monitored for 70 days. The purified enzyme exhibited proteolytic activity of 58.31 U/mL and collagenolytic activity of 28 U/mL, with a purification factor of 5.75-fold and a yield of 3.19%. The powdered forms, both lyophilized and spray-dried, showed greater stability, retaining approximately 68% and 86%, respectively, of residual activity after 70 days of storage. Additionally, a patent survey related to collagenases was conducted to map the global and national technological development of this enzyme. Initially, Derwent, Lens, USPTO, WIPO, Espacenet, and INPI databases were used. Based on the number of results obtained, the Derwent portal was selected to provide a global overview. An analysis using the INPI portal was also performed to assess national production. The results demonstrated a high concentration of patents in the biotechnological (3,584), pharmaceutical (1,671), and cosmetic (1,186) sectors, with leading companies standing out in the field. In the Brazilian context, a relatively low number of patent filings (49) was observed. Thus, it can be concluded that collagenase has high potential for veterinary applications; however, it remains underexplored scientifically. The production and stabilization of collagenolytic protease in powdered form reinforce the feasibility of its practical use, while the technological monitoring highlights that it is a strategic enzyme in the context of biotechnology and innovation.

COMMITTEE MEMBERS:
Presidente - TATIANA SOUZA PORTO
Externa à Instituição - LILIANA ANDREA DOS SANTOS - UFRPE
Externo à Instituição - THIAGO PAJEÚ NASCIMENTO - UFPI