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<p>Investment in research and development of alternative proteins has gained prominence in recent decades. In this scenario, the vegetable protein market stands out for using agro-industrial by-products, offering a sustainable and versatile alternative. Among these by-products is baru almond meal, obtained after mechanical pressing to extract the oil, which can contain ~ 33&#xa0;g/100&#xa0;g of protein. As a promising source of plant proteins, baru almond meal can be used as a substrate in the protein hydrolysis process to obtain bioactive peptides and/or protein hydrolysate, increasing its availability and bioactivity. The objective of this work was to study the enzymatic hydrolysis process of baru almond meal using the Alcalase enzyme, studying different proportions enzyme:substrate ratio (1%–3%), temperature (50–70&#xa0;°C), and pH (6.0–8.5) conditions, and evaluating technological and bioactive properties of the hydrolysates obtained. The results indicated different degrees of hydrolysis for the 17 assays evaluated (ranging from 1.15% to 28.60%), with some presenting good oil retention properties (230.18%) (assay 16) and emulsification capacity (134.7 m<sup>2</sup>/g) (assay 12). In addition to demonstrating expressive functional properties, six other assays (2, 3, 4, 13, 15, and 16) showed no significant difference in the five pH ranges analyzed for solubility. Considering all assays, the antioxidant potential is evidenced by inhibition of DPPH ≥ 53.76% and ABTS ≥ 88.87%. From the statistical analysis, assay 12 was selected as the optimal experiment, and its structural analysis indicated moderate colloidal stability through zeta potential and good thermal resistance. Assay 12 also presented good thermal properties, according to the structural evaluation, revealing great potential for application in different food processes, in sensory quality control, and as a substitute for synthetic agents.</p>

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Process conditions of enzymatic hydrolysis of baru (Dipteryx Alata Vogel) almond meal and technological and bioactive properties of protein hydrolysate

  • 期刊论文

  • 发表日期：

    2026年1月22日

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  • Isabelly de Campos Gonçalves Cabassa,
  • Gabrielly Silva Freitas,
  • Ana Carolina Alves Teles,
  • Sibele Santos Fernandes,
  • Mariana Buranelo Egea

摘要

Investment in research and development of alternative proteins has gained prominence in recent decades. In this scenario, the vegetable protein market stands out for using agro-industrial by-products, offering a sustainable and versatile alternative. Among these by-products is baru almond meal, obtained after mechanical pressing to extract the oil, which can contain ~ 33 g/100 g of protein. As a promising source of plant proteins, baru almond meal can be used as a substrate in the protein hydrolysis process to obtain bioactive peptides and/or protein hydrolysate, increasing its availability and bioactivity. The objective of this work was to study the enzymatic hydrolysis process of baru almond meal using the Alcalase enzyme, studying different proportions enzyme:substrate ratio (1%–3%), temperature (50–70 °C), and pH (6.0–8.5) conditions, and evaluating technological and bioactive properties of the hydrolysates obtained. The results indicated different degrees of hydrolysis for the 17 assays evaluated (ranging from 1.15% to 28.60%), with some presenting good oil retention properties (230.18%) (assay 16) and emulsification capacity (134.7 m2/g) (assay 12). In addition to demonstrating expressive functional properties, six other assays (2, 3, 4, 13, 15, and 16) showed no significant difference in the five pH ranges analyzed for solubility. Considering all assays, the antioxidant potential is evidenced by inhibition of DPPH ≥ 53.76% and ABTS ≥ 88.87%. From the statistical analysis, assay 12 was selected as the optimal experiment, and its structural analysis indicated moderate colloidal stability through zeta potential and good thermal resistance. Assay 12 also presented good thermal properties, according to the structural evaluation, revealing great potential for application in different food processes, in sensory quality control, and as a substitute for synthetic agents.