Antimicrobial and radical scavenging properties of bovine collagen hydrolysates produced by Penicillium aurantiogriseum URM 4622 collagenase.
Identifieur interne : 000231 ( Main/Exploration ); précédent : 000230; suivant : 000232Antimicrobial and radical scavenging properties of bovine collagen hydrolysates produced by Penicillium aurantiogriseum URM 4622 collagenase.
Auteurs : Carolina A. Lima ; Júlia Furtado Campos ; José L Lima Filho ; Attilio Converti [Italie] ; Maria G Carneiro Da Cunha ; Ana L F. PortoSource :
- Journal of food science and technology [ 0022-1155 ] ; 2015.
Abstract
A 2(3) full factorial design was used to identify the main effects and interactions of pH, collagen concentration and temperature on the degree of collagen hydrolysis (DH) by collagenase from Penicillium aurantiogriseum URM 4622. Increases in both pH and collagen concentration improved DH, and a positive interaction effect was observed for these variables. On the other hand, temperature had a negative main effect on DH. The maximum value of DH (4.65 μg/mL) was achieved at 7.5 mg/mL collagen concentration, pH 8.0 and 25 °C. The peptide profile showed several peptides with molecular weights lower than 2 kDa and exhibited antibacterial activity against Escherichia coli, Bacillus subtilis and Staphylococcus aureus. An antioxidant activity of 84.7 ± 0.24 % towards the radical ABTS• + was obtained with 50 mg/mL hydrolysates. This study demonstrated that collagen hydrolysed by P. aurantiogriseum URM 4622 collagenase possesses interesting antibacterial and antioxidant activities.
DOI: 10.1007/s13197-014-1463-y
PubMed: 26139912
Affiliations:
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Lima</name><affiliation><nlm:affiliation>Faculty of Science, Education and Technology of Garanhuns, University of Pernambuco-UPE, Av. Capitão Pedro Rodrigues, n 105, Garanhuns, PE Brazil.</nlm:affiliation><wicri:noCountry code="subField">PE Brazil</wicri:noCountry></affiliation></author><author><name sortKey="Campos, Julia Furtado" sort="Campos, Julia Furtado" uniqKey="Campos J" first="Júlia Furtado" last="Campos">Júlia Furtado Campos</name><affiliation><nlm:affiliation>Northeastern Center of Strategic Technologies (CETENE), Av. Prof. Luiz Freire, n 1, Recife, PE 50740-540 Brazil.</nlm:affiliation><wicri:noCountry code="subField">PE 50740-540 Brazil</wicri:noCountry></affiliation></author><author><name sortKey="Filho, Jose L Lima" sort="Filho, Jose L Lima" uniqKey="Filho J" first="José L Lima" last="Filho">José L Lima Filho</name><affiliation><nlm:affiliation>Laboratory of Immunopathology Keizo Asami (LIKA), Federal University of Pernambuco-UFPE, Av. Prof. Moraes Lins do Rego, s/n, Recife, PE 50670-901 Brazil ; Department of Biochemistry, Federal University of Pernambuco-UFPE, Av. 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Prof. Moraes Lins do Rego, s/n, Recife, PE 50670-901 Brazil ; Department of Biochemistry, Federal University of Pernambuco-UFPE, Av. Professor Moraes Rego, s/n, Campus Universitário, Recife, PE 50670-901 Brazil.</nlm:affiliation><wicri:noCountry code="subField">PE 50670-901 Brazil</wicri:noCountry></affiliation></author><author><name sortKey="Porto, Ana L F" sort="Porto, Ana L F" uniqKey="Porto A" first="Ana L F" last="Porto">Ana L F. Porto</name><affiliation><nlm:affiliation>Laboratory of Immunopathology Keizo Asami (LIKA), Federal University of Pernambuco-UFPE, Av. Prof. Moraes Lins do Rego, s/n, Recife, PE 50670-901 Brazil ; Department of Morphology and Animal Physiology, Federal Rural University of Pernambuco-UFRPE, Av. 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The maximum value of DH (4.65 μg/mL) was achieved at 7.5 mg/mL collagen concentration, pH 8.0 and 25 °C. The peptide profile showed several peptides with molecular weights lower than 2 kDa and exhibited antibacterial activity against Escherichia coli, Bacillus subtilis and Staphylococcus aureus. An antioxidant activity of 84.7 ± 0.24 % towards the radical ABTS• + was obtained with 50 mg/mL hydrolysates. 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Porto</name></noCountry><country name="Italie"><noRegion><name sortKey="Converti, Attilio" sort="Converti, Attilio" uniqKey="Converti A" first="Attilio" last="Converti">Attilio Converti</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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