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Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives

Kenaf seeds are a promising source of natural preservatives for food applications due to their potential as a substrate to generate peptides with high antibacterial activity. We sought to generate bioactive peptides with antibacterial activity from Kenaf seed proteins via lacto-fermentation. The gro...

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Main Authors: Arulrajah, Brisha, Muhialdin, Belal J., Zarei, Mohammad, Hasan, Hanan, Saari, Nazamid
Format: Article
Language:English
Published: Elsevier 2020
Online Access:http://psasir.upm.edu.my/id/eprint/89541/1/KENAF.pdf
http://psasir.upm.edu.my/id/eprint/89541/
https://www.sciencedirect.com/science/article/pii/S0956713519305584
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spelling my.upm.eprints.895412021-08-16T10:15:31Z http://psasir.upm.edu.my/id/eprint/89541/ Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives Arulrajah, Brisha Muhialdin, Belal J. Zarei, Mohammad Hasan, Hanan Saari, Nazamid Kenaf seeds are a promising source of natural preservatives for food applications due to their potential as a substrate to generate peptides with high antibacterial activity. We sought to generate bioactive peptides with antibacterial activity from Kenaf seed proteins via lacto-fermentation. The ground seeds were defatted and protein extracted using acid precipitation. Kenaf seed protein was fermented with Lactobacillus casei for 72 h at 37 °C, and the antibacterial activity, MIC, and MBC were determined using a 96-well microtiter plate assay. The fermented protein was subjected to fractionation and peptide identification using reversed-phase high pressure liquid chromatography and liquid chromatography-mass spectrometry, respectively. The fermented protein showed high antibacterial activity against Salmonella typhimurim, Escherichia coli, Psedomonas aerginosa, Staphylococcus aureus, Bacilus subtilis, and Streptococcus pyogenes. The MIC value was 4 mg/mL against all tested pathogens and the MBC value was 8 mg/mL against S. typhimurium, P. aureginosa, and E. coli and 4 mg/mL against B. subtilis, S. aureus, and S. pyogenes. Fraction 17 demonstrated the strongest antibacterial activity (98%–100%), and five peptides sequences were identified in this fraction. The findings of this study demonstrated high potential for kenaf seed protein fermented using Lactobacillus casei as a source of natural preservatives for a broad range of food applications. Elsevier 2020-04 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/89541/1/KENAF.pdf Arulrajah, Brisha and Muhialdin, Belal J. and Zarei, Mohammad and Hasan, Hanan and Saari, Nazamid (2020) Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives. Food Control, 110. pp. 1-6. ISSN 0956-7135 https://www.sciencedirect.com/science/article/pii/S0956713519305584 10.1016/j.foodcont.2019.106969
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description Kenaf seeds are a promising source of natural preservatives for food applications due to their potential as a substrate to generate peptides with high antibacterial activity. We sought to generate bioactive peptides with antibacterial activity from Kenaf seed proteins via lacto-fermentation. The ground seeds were defatted and protein extracted using acid precipitation. Kenaf seed protein was fermented with Lactobacillus casei for 72 h at 37 °C, and the antibacterial activity, MIC, and MBC were determined using a 96-well microtiter plate assay. The fermented protein was subjected to fractionation and peptide identification using reversed-phase high pressure liquid chromatography and liquid chromatography-mass spectrometry, respectively. The fermented protein showed high antibacterial activity against Salmonella typhimurim, Escherichia coli, Psedomonas aerginosa, Staphylococcus aureus, Bacilus subtilis, and Streptococcus pyogenes. The MIC value was 4 mg/mL against all tested pathogens and the MBC value was 8 mg/mL against S. typhimurium, P. aureginosa, and E. coli and 4 mg/mL against B. subtilis, S. aureus, and S. pyogenes. Fraction 17 demonstrated the strongest antibacterial activity (98%–100%), and five peptides sequences were identified in this fraction. The findings of this study demonstrated high potential for kenaf seed protein fermented using Lactobacillus casei as a source of natural preservatives for a broad range of food applications.
format Article
author Arulrajah, Brisha
Muhialdin, Belal J.
Zarei, Mohammad
Hasan, Hanan
Saari, Nazamid
spellingShingle Arulrajah, Brisha
Muhialdin, Belal J.
Zarei, Mohammad
Hasan, Hanan
Saari, Nazamid
Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives
author_facet Arulrajah, Brisha
Muhialdin, Belal J.
Zarei, Mohammad
Hasan, Hanan
Saari, Nazamid
author_sort Arulrajah, Brisha
title Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives
title_short Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives
title_full Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives
title_fullStr Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives
title_full_unstemmed Lacto-fermented Kenaf (Hibiscus cannabinus L.) seed protein as a source of bioactive peptides and their applications as natural preservatives
title_sort lacto-fermented kenaf (hibiscus cannabinus l.) seed protein as a source of bioactive peptides and their applications as natural preservatives
publisher Elsevier
publishDate 2020
url http://psasir.upm.edu.my/id/eprint/89541/1/KENAF.pdf
http://psasir.upm.edu.my/id/eprint/89541/
https://www.sciencedirect.com/science/article/pii/S0956713519305584
_version_ 1709669020797501440
score 13.211869

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