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Bioactive properties of protein hydrolysate of cottonseed byproduct: antioxidant, antimicrobial, and angiotensin‐converting enzyme (ACE) inhibitory activity
Author(s) -
Egea Mariana Buranelo,
de Oliveira Filho Josemar Gonçalves,
Lemes Ailton Cesar,
Valencia-Mejia Erika,
Fernandes Katia Flavia,
de Figueiredo Sousa Heloisa Alves,
da Silva Edilsa Rosa,
Dyszy Fábio H.
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.07067
Subject(s) - hydrolysate , chemistry , cottonseed , antioxidant , cottonseed meal , dpph , hydrolysis , chromatography , enzymatic hydrolysis , enzyme , food science , biochemistry , soybean meal , organic chemistry , raw material
Cottonseed meal is a byproduct generated in large amounts resulting from the process of extracting cottonseed oil. The aim of this study was to investigate the cottonseed byproduct hydrolysate produced with Alcalase ® (A), Neutrase ® (N), or Flavourzyme ® (F), and thus, evaluate its the antioxidant activity and angiotensin‐converting enzyme (ACE) inhibitory activity, as well as ability to inhibit the strains of Staphylococcus aureus, and Escherichia coli . The protein hydrolysates (PH) were obtained using thermal pretreatment (CT – control and HT – thermal pretreatment) and enzymatic hydrolysis of protein extract obtained of cottonseed byproduct. The decreasing order of the degree of hydrolysis of protein hydrolysate: HT‐A>CT‐A>HT‐N>CT‐N>HT‐F>CT‐F. The DPPH scavenging activity of the hydrolysates obtained from the Alcalase ® , Neutrase ® , and Flavourzyme ® treatments at the end of the reaction (100 min) were 95.44%, 78.10%, and 62.94% for the HT hydrolysates, respectively, and 88.60%, 70.69%, and 62.06% for the CT hydrolysates, respectively. The ferric reducing antioxidant power of the hydrolysates obtained from the Alcalase ® , Neutrase ® , and Flavourzyme ® treatments at the end of the reaction were 0.47, 0.44, and 0.34 mg TE/mg sample for the HT hydrolysates, respectively, and 0.38, 0.43, and 0.28 mg TE/mg for the CT hydrolysates, respectively. The results of the growth inhibition of S. aureus obtained from the Alcalase ® , Neutrase ® , and Flavourzyme ® treatments at the end of the reaction were 32.38%, 16.66%, and 22.35 for the HT hydrolysates, respectively, and 28.35%, 16.68%, and 17.85% for the CT hydrolysates, respectively. The heat‐pretreated hydrolysates were able to inhibit the growth of S. aureus . The growth inhibition of E. coli was lower when compared to that of S. aureus . The growth was inhibited from 13 to 18 % and was observed for the HT hydrolysates produced using Alcalase ® after 20 min of reaction. The hydrolysates showed ACE inhibition of 74 to 99 %. The hydrolysate produced using Alcalase ® with thermal treatment showed higher antioxidant activity and ACE inhibition (99.5%) than other enzymes. In this study, it was possible to obtain PH with different bioactivity properties using adequate processing by successfully choosing proteolytic enzymes and thermally pretreating proteins from the cottonseed byproduct. Support or Funding Information This work was supported of the FAPEG (Process 201610267000530), CAPES (001), CNPq (06/2016), IFB (030/2016) and IF Goiano (Process 23218.000788/2018‐41).