Dados do Trabalho

Título

FOUND ANTIOXIDANT ACTIVITY IN PROTEIN HYDROLYSATE RICH IN PEPTIDES FROM MURUMURU (Astrocaryum Murumuru) BIOMASS

Introdução

Amazon Forest has a large biodiversity of valuable inputs that contribute for the bioeconomy of the region, among them, the oilseeds murumuru (Astrocaryum murumuru), which is most used for oil extraction. From this process, a valuable residue designated as biomass that is improperly discarded in the environment, this material is rich in bioactive compounds, such as phenolic compounds, flavonoids and peptides that can improve the health with their beneficial actions.

Material e Métodos

The aim of this work was obtaining peptides from protein hydrolysates from murumuru biomass and evaluate their antioxidant activity. The protein extraction was carried out using a mass/volume ratio of 1:10 for 60 minutes at pH of 10.0, followed of the isoelectric precipitation at pH 4.5. Two different methods were used to obtain the protein hydrolysate: 1-alcalase enzyme (≥ 0.75 Anson units/mL activity) from Bacillus licheniformis in PBS buffer with pH adjusted to 8.5, temperature adjusted to 50 °C, and enzyme/substrate (E/S) ratios of 1:50, 1:100, and 1:200 with a hydrolysis time of three hours; 2-commercial trypsin enzyme in water with pH adjusted to 7.5, 37 °C for 24 hours under the same conditions of E/S ratio for alcalase. The resultant hydrolysate was centrifuged at 10,000×g for 20 minutes after being heated at 100 °C, an ice bath was used in order to inactive the enzyme. High performance liquid chromatography was utilized to define the peptide peaks of the protein hydrolysates, the DPPH and ABTS procedures were employed to measure the activity antioxidant (AC), and the Lowry method was used to calculate the protein content of the hydrolysate.

Resultados e Discussão

For alcalase and trypsin, the optimal hydrolysis conditions were an E/S ratio of 1:200 and 1:50, respectively, producing a hydrolysate with about 31% and 41% protein, respectively. Trypsin hydrolysate yielded the highest AC, displaying ~473 DPPH µM TE and ~2,344 ABTS µM TE g/protein; alcalase hydrolysate yielded ~139 DPPH µM TE and ~1,899 ABTS µM TE g/protein.

Conclusão

This study was pioneering in obtaining murumuru biomass peptides and its antioxidant activity, showing that this residue can be valued and used as a high-value-added byproduct as bioactive peptides that can be applied fine chemistry.