Dados do Trabalho

Título

OBTAINING HYDROLYSATE RICH IN PEPTIDES FROM ANDIROBA (Carapa guianensis) BIOMASS WITH HIGH ANTIOXIDANT ACTIVITY

Introdução

Andiroba (Carapa guianensis) seeds contain significant amounts of fatty acids, fiber, phenolic compounds, among other chemical compounds capable of exerting various actions that bring health benefits. The oil is extracted for the local bioeconomy and therapeutic, medicinal and cosmetic purposes, generating biomass discarded in the environment. This residue has bioactive compounds in its composition with great potential for exploration, such as its protein fraction. Plant proteins, when hydrolysed, can release bioactive peptides encrypted in its structure that can present physiological functionalities, including antioxidant activity. This study aimed obtaining peptide-rich hydrolysates from andiroba biomass through its protein isolate and evaluate its antioxidant capacity (AC).

Material e Métodos

The protein of andiroba biomass was extracted in these conditions: mass/volume ratio of 1:10 for 60 minutes with pH adjusted to 10.0 followed by isoelectric precipitation at pH 4.5. two methods were used for obtaining protein hydrolysates: 1- alcalase enzyme from Bacillus licheniformis (≥ 0.75 Anson units/mL activity) in PBS buffer with pH adjusted in 8.5, temperature of the 50 °C, and enzyme/substrate (E/S) ratio 1:50, 1:100, and 1:200 and hydrolysis time of 3 hours and, 2- commercial trypsin enzyme in water with pH adjusted in 7.5, 37°C for 24h on same conditions of E/S ratio for alcalase. The resulting supernatant was collected, freeze-dried, and stored at -18°C. The hydrolysate protein content was determined by the Lowry method. High performance liquid chromatography was used to characterize the peptide peaks of the protein hydrolysates and, AC measured by the DPPH and ABTS methods.

Resultados e Discussão

The best hydrolysis conditions were using the E/S ratio of 1:100 for alcalase and 1:50 for trypsin enzymes, resulting in a hydrolysate with ~28 and 46% protein, respectively. The highest AC was obtained for the hydrolysate with alcalase, presenting ~524 DPPH UM TE g/protein and, ~4,160 ABTS UM TE g/protein, while the AC for the tryptic hydrolysate was ~371 DPPH UM TE g/protein and, ~2,567 ABTS UM TE g/protein.

Conclusão

This study is the first reported in the literature to obtain peptides with high antioxidant activity, which were obtained from the residue of an Amazonian oilseed, demonstrating that andiroba biomass can be exploited to generate bio-inputs.