Effects of enzymatic hydrolysis (Flavourzyme®) assisted by ultrasound in the structural and functional properties of hydrolyzates from different bovine collagens

Vidal, Alessandra Roseline; Ferreira, Thaísa Egiéli; Mello, Renius; Schmidt, Michele M.; Kubota, Ernesto Hashime; Demiate, Ivo Mottin; Zielinski, Acácio Antônio Ferreira; Dornelles, Rosa Cristina Prestes

doi:10.1590/fst.16717

Cited by 18 publications

(14 citation statements)

References 27 publications

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“…Flavourzyme  is a complex fungal protease produced by the submerged fermentation of a selected lineage of Aspergillus oryzae which has not been genetically modified; it is used in neutral or slightly acidic conditions (Šližyte et al, 2005). On a study by Vidal et al (2018) enzymatic hydrolysis, with Flavourzyme  , provided structural rupture and improved the functionality to the different bovine collagen hydrolysates.…”

Section: Introductionmentioning

confidence: 99%

Characterization of hydrolysates of collagen from mechanically separated chicken meat residue

et al. 2020

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Dbtaining collagen and hydrolysates from mechanically separated chicken meat residue is an excellent way to add value to this waste. The aims of this study were to obtain collagen hydrolysates from chicken MSM residue using Alcalase  and Flavourzyme  enzymes, as well characterizing the functional, structural and thermal stability properties. The highest degree of hydrolysis was obtained using Alcalase  , 36.11%, while using Flavourzyme  resulted in 12.02%. The DSC analysis of the collagen indicated a denaturation temperature of 46.47 °C. The FTOR spectra of the crude collagen showed absorption peaks that were characteristic of amide bands A, B, O, OO and OOO. On the spectra of the hydrolysed the area of the amide bands was reduced, and some peaks appeared between 800 and 1,200 cm-1. The disappearance of high molecular weight bands in the SDS-PAGE analysis also confirmed the hydrolysis of collagen. After the hydrolysis, the collagen presented reduced viscosity, the capacity to form foam, and foam stability. The emulsifying activity index was high in the hydrolysates in relation to the crude collagen. Thus, the use of Alcalase  and Flavourzyme  to obtain hydrolysates from collagen derived from chicken MSM residue was shown to be viable, and potentially useful for industrial applications.

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Section: Introductionmentioning

confidence: 99%

Characterization of hydrolysates of collagen from mechanically separated chicken meat residue

et al. 2020

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“…Several studies on antioxidant activity have been conducted with HC from different sources such as pigs [4,21], cows [22], fish [23,24,25], and invertebrates like jellyfishes or sponges [26,27]. However, less is known about the properties of hydrolysed collagen extracted from ovine sources and its possible applications.…”

Section: Introductionmentioning

confidence: 99%

Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity

León-López

Fuentes-Jiménez

Hernández-Fuentes

et al. 2019

IJMS

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The extraction and enzymatic hydrolysis of collagen from sheepskins at different times of hydrolysis (0, 10, 15, 20, 30 min, 1, 2, 3 and 4 h) were investigated in terms of amino acid content (hydroxyproline), isoelectric point, molecular weight (Mw) by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method, viscosity, Fourier-transform infrared (FTIR) spectroscopy, antioxidant capacity by 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) assays, thermal properties (Differential Scanning Calorimetry) and morphology by scanning electron microscopy (SEM) technique. The kinetics of hydrolysis showed an increase in the protein and hydroxyproline concentration as the hydrolysis time increased to 4 h. FTIR spectra allowed us to identify the functional groups of hydrolysed collagen (HC) in the amide I region for collagen. The isoelectric point shifted to lower values compared to the native collagen precursor. The change in molecular weight and viscosity from time 0 min to 4 h promoted important antioxidant activity in the resulting HC. The lower the Mw, the greater the ability to donate an electron or hydrogen to stabilize radicals. From the SEM images it was evident that HC after 2 h had a porous and spongy structure. These results suggest that HC could be a good alternative to replace HC from typical sources like pigs, cows and fish.

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“…By enzymatic hydrolysis, using plant or animal proteases, protein hydrolysates can be obtained from by-products. Enzymatic hydrolysis can modify several functional groups and is used to increase the functionality of proteins through structural modification [ 9 , 10 , 11 , 12 , 13 , 14 , 15 ]. One of the enzymes most commonly used in the process of collagen hydrolysis is Alcalase ® , which can be used at high temperatures, moderate alkalinity [ 16 ], and enable a cleaner hydrolysis process.…”

Section: Introductionmentioning

confidence: 99%

Production of Collagens and Protein Hydrolysates with Antimicrobial and Antioxidant Activity from Sheep Slaughter By-Products

et al. 2022

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This work aimed to produce collagens and hydrolysates with antimicrobial and antioxidant activity from sheep slaughter by-products. The by-products (sheep and lamb) were treated and extracted. The collagens were hydrolyzed with the enzyme Alcalase®. The spectra of collagens and hydrolysates were similar (amide bands I, II, III, A, B). The bands presented by the collagens (α1, α2, β) were characteristic of type I collagen. The hydrolysates showed molecular weight peptides equal to/lower than 15 kDa. Collagens had a denaturation temperature of 39.32 (lamb) and 36.38 °C (sheep), whereas the hydrolysates did not undergo thermal transition. Hydrolysates showed lower values of antioxidant activity (AA) than the collagens. The collagens from lamb and from sheep displayed an AA of 13.4% (concentration of 0.0002%) and 13.1% (concentration of 0.0005%), respectively. At the concentration of 0.0020%, the lamb hydrolysates displayed an AA of 10.2%, whereas the sheep hydrolysates had an AA of only 1.98%. Collagen also showed higher antimicrobial activity compared to hydrolysates, requiring a lower concentration to inhibit the microorganisms tested. Sheep slaughter by-products proved to be a viable source for obtaining protein hydrolysates and collagens with antimicrobial and antioxidant activity, which can be applied in the development of nutraceuticals beneficial to human health.

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Effects of enzymatic hydrolysis (Flavourzyme®) assisted by ultrasound in the structural and functional properties of hydrolyzates from different bovine collagens

Cited by 18 publications

References 27 publications

Characterization of hydrolysates of collagen from mechanically separated chicken meat residue

Characterization of hydrolysates of collagen from mechanically separated chicken meat residue

Hydrolysed Collagen from Sheepskins as a Source of Functional Peptides with Antioxidant Activity

Production of Collagens and Protein Hydrolysates with Antimicrobial and Antioxidant Activity from Sheep Slaughter By-Products

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