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Int. J. Mol. Sci. 2012, 13(12), 16796-16811; doi:10.3390/ijms131216796
Article

Actinopyga lecanora Hydrolysates as Natural Antibacterial Agents

1
, 1
, 1
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 and 1,*
Received: 25 October 2012; Accepted: 1 December 2012 / Published: 7 December 2012
(This article belongs to the Section Bioactives and Nutraceuticals)
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Abstract: Actinopyga lecanora, a type of sea cucumber commonly known as stone fish with relatively high protein content, was explored as raw material for bioactive peptides production. Six proteolytic enzymes, namely alcalase, papain, pepsin, trypsin, bromelain and flavourzyme were used to hydrolyze A. lecanora at different times and their respective degrees of hydrolysis (DH) were calculated. Subsequently, antibacterial activity of the A. lecanora hydrolysates, against some common pathogenic Gram positive bacteria (Bacillus subtilis and Staphylococcus aureus) and Gram negative bacteria (Escherichia coli, Pseudomonas aeruginosa, and Pseudomonas sp.) were evaluated. Papain hydrolysis showed the highest DH value (89.44%), followed by alcalase hydrolysis (83.35%). Bromelain hydrolysate after one and seven hours of hydrolysis exhibited the highest antibacterial activities against Pseudomonas sp., P. aeruginosa and E. coli at 51.85%, 30.07% and 30.45%, respectively compared to the other hydrolysates. Protein hydrolysate generated by papain after 8 h hydrolysis showed maximum antibacterial activity against S. aureus at 20.19%. The potent hydrolysates were further fractionated using RP-HPLC and antibacterial activity of the collected fractions from each hydrolysate were evaluated, wherein among them only three fractions from the bromelain hydrolysates exhibited inhibitory activities against Pseudomonas sp., P. aeruginosa and E. coli at 24%, 25.5% and 27.1%, respectively and one fraction of papain hydrolysate showed antibacterial activity of 33.1% against S. aureus. The evaluation of the relationship between DH and antibacterial activities of papain and bromelain hydrolysates revealed a meaningful correlation of four and six order functions.
Keywords: Actinopyga lecanora; bioactive peptides; antibacterial activity; proteolytic enzyme Actinopyga lecanora; bioactive peptides; antibacterial activity; proteolytic enzyme
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Ghanbari, R.; Ebrahimpour, A.; Abdul-Hamid, A.; Ismail, A.; Saari, N. Actinopyga lecanora Hydrolysates as Natural Antibacterial Agents. Int. J. Mol. Sci. 2012, 13, 16796-16811.

AMA Style

Ghanbari R, Ebrahimpour A, Abdul-Hamid A, Ismail A, Saari N. Actinopyga lecanora Hydrolysates as Natural Antibacterial Agents. International Journal of Molecular Sciences. 2012; 13(12):16796-16811.

Chicago/Turabian Style

Ghanbari, Raheleh; Ebrahimpour, Afshin; Abdul-Hamid, Azizah; Ismail, Amin; Saari, Nazamid. 2012. "Actinopyga lecanora Hydrolysates as Natural Antibacterial Agents." Int. J. Mol. Sci. 13, no. 12: 16796-16811.



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