Partial purification and characterization of bioactive peptides derived from New Zealand green-lipped mussels (Perna canaliculus) protein hydrolysates.

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dc.contributor.advisor Perera, CO en
dc.contributor.author Jayaprakash, Ramya en
dc.date.accessioned 2016-10-19T20:13:17Z en
dc.date.issued 2016 en
dc.identifier.uri http://hdl.handle.net/2292/30809 en
dc.description Full text is available to authenticated members of The University of Auckland only. en
dc.description.abstract Marine-derived bioactive peptides produced by enzymatic hydrolysis are the main focus of contemporary research. These bioactive peptides are emerging as a promising therapeutic tool for preventing or controlling various diseases due to their potential role in exerting innumerable biological activities including, antioxidant, antihypertensive, antimicrobial, opioid activities and so on. This study was aimed to explore the bioactive peptides released from New Zealand green-lipped mussels (Perna canaliculus) through enzymatic hydrolysis and their biological properties. NZ green-lipped mussel protein was prepared from fresh and live green-lipped mussels and hydrolysed for 240 min using two different commercial enzymes namely, pepsin and alcalase. Protein hydrolysates collected at different time intervals (30, 60, 90, 120, 150, 180, 210, 240 min) from pepsin and alcalase hydrolysis reaction was evaluated to determine the extent of hydrolysis took place. In both cases, the results showed that the optimum time in which maximum amount of proteins hydrolysed was at 30 min and no apparent hydrolysis took place up to 240 min hydrolysis. In addition, antioxidant and ACE inhibitory activities of each protein hydrolysates were investigated. The results indicated that the pepsin hydrolysate with 30min hydrolysis, named as GPH, exhibited the highest antioxidant activity with 82 ± 0.08% against DPPH (2, 2-Diphenyl-1-picrylhydrazyl) radicals, 77 ± 0.037% against ABTS (2, 2’-azino-bis-ethylbenzthiazoline-6-sulfonic acid) radicals and also 95 ± 2.54% of ACE inhibitory activity, among other protein hydrolysates. GPH was tested further for antimicrobial activity and no positive result was observed indicating the presence of antimicrobial peptides in the protein hydrolysate. Purification of GPH using gel-filtration chromatography revealed that the particular protein fraction (GPH-IV*), containing peptides with molecular weight (MW) below 5 kDa had the strongest antioxidant and ACE inhibitory activities but no antimicrobial activity was observed. By using Reversed Phase HPLC (RP-HPLC), bioactive peptide fraction (GPH-IV*) was purified and observed that peak 2 (GPH-IV*-P2) had the strongest antioxidant and ACE inhibitory activity. Finally, several bioactive peptides with MW (~1 kDa) were identified from peak 2 (GPH-IV*-P2) using LC-MS and in silico analysis. From this study, it has been analysed that green-lipped mussel protein hydrolysates could be used as a good source of bioactive peptides with different therapeutic applications. en
dc.publisher ResearchSpace@Auckland en
dc.relation.ispartof Masters Thesis - University of Auckland en
dc.relation.isreferencedby UoA99206757814002091 en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. en
dc.rights Restricted Item. Available to authenticated members of The University of Auckland. en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/3.0/nz/ en
dc.title Partial purification and characterization of bioactive peptides derived from New Zealand green-lipped mussels (Perna canaliculus) protein hydrolysates. en
dc.type Thesis en
thesis.degree.discipline Food Science en
thesis.degree.grantor The University of Auckland en
thesis.degree.level Masters en
dc.rights.holder Copyright: The author en
pubs.elements-id 543031 en
pubs.record-created-at-source-date 2016-10-20 en


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