Co-production of Proteases and Bioactive Protein Hydrolysates from Bioprocessing of Feather Meal

Bernardo, Bernardete da Silva; Ramos, Rodrigo Ferraz; Callegaro, Kelly; Daroit, Daniel Joner

doi:10.1590/1678-4324-2019180621

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Article - Agriculture, Agribusiness and Biotechnology • Braz. Arch. Biol. Technol. 62 • 2019 • https://doi.org/10.1590/1678-4324-2019180621 linkcopy

Co-production of Proteases and Bioactive Protein Hydrolysates from Bioprocessing of Feather Meal

Authorship SCIMAGO INSTITUTIONS RANKINGS

Feather meal conversion through submerged cultivations with Bacillus strains (CL33A, CL14) yielded proteases and protein hydrolysates. After 4-day (CL33A) and 10-day (CL14) cultivations, protease activities reached 461 U/mL; hydrolysates presented antioxidant (radicals-scavenging, 57-77%; Fe²⁺-chelation, 14-28%; Fe³⁺-reduction) and antidiabetic (dipeptidyl peptidase-IV inhibition, 49-52%) potentials. The obtained bioproducts present prospective commercial/industrial applications.

Keywords:
Bacillus; bioprocess; enzyme; antioxidant; antidiabetic

Authorship

person Bernardete da Silva Bernardo

schoolFederal University of Fronteira Sul (UFFS), Cerro Largo, RS, Brazil.Federal University of Fronteira SulBrazilCerro Largo, RS, BrazilFederal University of Fronteira Sul (UFFS), Cerro Largo, RS, Brazil.

0000-0001-7949-7141

person Rodrigo Ferraz Ramos

0000-0002-6414-376X

person Kelly Callegaro

0000-0003-2386-5130

person Daniel Joner Daroit *

0000-0001-5469-5766

person*Correspondence:
djdaroit@gmail.com; Tel.: +55-55-33594234 (D.J.D.)

Conflicts of Interest: The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.

SCIMAGO INSTITUTIONS RANKINGS

Federal University of Fronteira Sul (UFFS), Cerro Largo, RS, Brazil.Federal University of Fronteira SulBrazilCerro Largo, RS, BrazilFederal University of Fronteira Sul (UFFS), Cerro Largo, RS, Brazil.

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Figure 1 Feather meal degradation (●, %), protease production (■, U/mL), and soluble protein concentration (○, mg/mL) during submerged cultivations with Bacillus sp. CL33A (a) and Bacillus sp. CL14 (b) on feather meal broth. Data points are means ± standard deviation of experiments performed in triplicates. Different lowercase letters indicate significant differences (P < 0.05) within each evaluated parameter.

Thumbnail

Figure 2 Antioxidant potential, as assessed through the scavenging of DPPH radicals (●, %) and ABTS radicals (○, %), of feather meal hydrolysates produced by Bacillus sp. CL33A (a) and Bacillus sp. CL14 (b) during submerged cultivations on feather meal broth. Data points are means ± standard deviation of experiments performed in triplicates. Different lowercase letters indicate significant differences (P < 0.05) within each evaluated parameter.

Thumbnail

Figure 3 Antioxidant potential, as assessed through reducing power (○, A₇₀₀) and Fe²⁺-chelating ability (●, %), of feather meal hydrolysates produced by Bacillus sp. CL33A (a) and Bacillus sp. CL14 (b) during submerged cultivations on feather meal broth. Data points are means ± standard deviation of experiments performed in triplicates. Different lowercase letters indicate significant differences (P < 0.05) within each evaluated parameter.

Thumbnail

Figure 4 Inhibition of DPP IV activity (%) by feather meal hydrolysates produced by Bacillus sp. CL33A (a) and Bacillus sp. CL14 (b) during submerged cultivations on feather meal broth. Each column represents the mean ± standard deviation of experiments performed in triplicates. Different lowercase letters indicate significant differences (P < 0.05).

imageFigure 1 Feather meal degradation (●, %), protease production (■, U/mL), and soluble protein concentration (○, mg/mL) during submerged cultivations with Bacillus sp. CL33A (a) and Bacillus sp. CL14 (b) on feather meal broth. Data points are means ± standard deviation of experiments performed in triplicates. Different lowercase letters indicate significant differences (P < 0.05) within each evaluated parameter. open_in_new

imageFigure 2 Antioxidant potential, as assessed through the scavenging of DPPH radicals (●, %) and ABTS radicals (○, %), of feather meal hydrolysates produced by Bacillus sp. CL33A (a) and Bacillus sp. CL14 (b) during submerged cultivations on feather meal broth. Data points are means ± standard deviation of experiments performed in triplicates. Different lowercase letters indicate significant differences (P < 0.05) within each evaluated parameter. open_in_new

imageFigure 3 Antioxidant potential, as assessed through reducing power (○, A₇₀₀) and Fe²⁺-chelating ability (●, %), of feather meal hydrolysates produced by Bacillus sp. CL33A (a) and Bacillus sp. CL14 (b) during submerged cultivations on feather meal broth. Data points are means ± standard deviation of experiments performed in triplicates. Different lowercase letters indicate significant differences (P < 0.05) within each evaluated parameter. open_in_new

imageFigure 4 Inhibition of DPP IV activity (%) by feather meal hydrolysates produced by Bacillus sp. CL33A (a) and Bacillus sp. CL14 (b) during submerged cultivations on feather meal broth. Each column represents the mean ± standard deviation of experiments performed in triplicates. Different lowercase letters indicate significant differences (P < 0.05). open_in_new

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