Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana
Abstract Chlorella sorokiniana protein isolates were enzymatically hydrolyzed using pepsin, bromelain, and thermolysin, with their molecular characteristics and bioactivities determined. Thermolysin hydrolysates exhibited the highest degree of hydrolysis (18.08% ± 1.13%). The sodium dodecyl sulfate–...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Wiley
2019-07-01
|
Series: | Food Science & Nutrition |
Subjects: | |
Online Access: | https://doi.org/10.1002/fsn3.1097 |
_version_ | 1797221353445654528 |
---|---|
author | Lhumen A. Tejano Jose P. Peralta Encarnacion Emilia S. Yap Yu‐Wei Chang |
author_facet | Lhumen A. Tejano Jose P. Peralta Encarnacion Emilia S. Yap Yu‐Wei Chang |
author_sort | Lhumen A. Tejano |
collection | DOAJ |
description | Abstract Chlorella sorokiniana protein isolates were enzymatically hydrolyzed using pepsin, bromelain, and thermolysin, with their molecular characteristics and bioactivities determined. Thermolysin hydrolysates exhibited the highest degree of hydrolysis (18.08% ± 1.13%). The sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) results showed that peptides with molecular weights <10 kDa were found in the hydrolysates compared to the protein isolates. Bioactivity assays revealed that pepsin peptide fraction <5 kDa showed the highest angiotensin‐converting enzyme (ACE)‐inhibitory (34.29% ± 3.45%) and DPPH radical scavenging activities (48.86% ± 1.95%), while pepsin peptide fraction <10 kDa demonstrated the highest reducing power with 0.2101% ± 0.02% absorbance. Moreover, antibacterial assessment revealed that pepsin hydrolysate and peptide fractions displayed inhibition to the test microorganisms. Overall, the present findings suggest that C. sorokiniana protein hydrolysates can be valuable bio‐ingredients with pharmaceutical and nutraceutical application potentials. |
first_indexed | 2024-04-24T13:04:05Z |
format | Article |
id | doaj.art-7e9ecd131ee343feb29f08951b2ab8d3 |
institution | Directory Open Access Journal |
issn | 2048-7177 |
language | English |
last_indexed | 2024-04-24T13:04:05Z |
publishDate | 2019-07-01 |
publisher | Wiley |
record_format | Article |
series | Food Science & Nutrition |
spelling | doaj.art-7e9ecd131ee343feb29f08951b2ab8d32024-04-05T09:16:22ZengWileyFood Science & Nutrition2048-71772019-07-01772381239010.1002/fsn3.1097Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokinianaLhumen A. Tejano0Jose P. Peralta1Encarnacion Emilia S. Yap2Yu‐Wei Chang3College of Fisheries and Ocean Sciences, Institute of Fish Processing Technology University of the Philippines Visayas Miagao Iloilo PhilippinesCollege of Fisheries and Ocean Sciences, Institute of Fish Processing Technology University of the Philippines Visayas Miagao Iloilo PhilippinesCollege of Fisheries and Ocean Sciences, Institute of Fish Processing Technology University of the Philippines Visayas Miagao Iloilo PhilippinesDepartment of Food Science National Taiwan Ocean University Keelung TaiwanAbstract Chlorella sorokiniana protein isolates were enzymatically hydrolyzed using pepsin, bromelain, and thermolysin, with their molecular characteristics and bioactivities determined. Thermolysin hydrolysates exhibited the highest degree of hydrolysis (18.08% ± 1.13%). The sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) results showed that peptides with molecular weights <10 kDa were found in the hydrolysates compared to the protein isolates. Bioactivity assays revealed that pepsin peptide fraction <5 kDa showed the highest angiotensin‐converting enzyme (ACE)‐inhibitory (34.29% ± 3.45%) and DPPH radical scavenging activities (48.86% ± 1.95%), while pepsin peptide fraction <10 kDa demonstrated the highest reducing power with 0.2101% ± 0.02% absorbance. Moreover, antibacterial assessment revealed that pepsin hydrolysate and peptide fractions displayed inhibition to the test microorganisms. Overall, the present findings suggest that C. sorokiniana protein hydrolysates can be valuable bio‐ingredients with pharmaceutical and nutraceutical application potentials.https://doi.org/10.1002/fsn3.1097angiotensin‐converting enzyme inhibitoryantibacterial activityantioxidant activityChlorella sorokiniana |
spellingShingle | Lhumen A. Tejano Jose P. Peralta Encarnacion Emilia S. Yap Yu‐Wei Chang Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana Food Science & Nutrition angiotensin‐converting enzyme inhibitory antibacterial activity antioxidant activity Chlorella sorokiniana |
title | Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana |
title_full | Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana |
title_fullStr | Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana |
title_full_unstemmed | Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana |
title_short | Bioactivities of enzymatic protein hydrolysates derived from Chlorella sorokiniana |
title_sort | bioactivities of enzymatic protein hydrolysates derived from chlorella sorokiniana |
topic | angiotensin‐converting enzyme inhibitory antibacterial activity antioxidant activity Chlorella sorokiniana |
url | https://doi.org/10.1002/fsn3.1097 |
work_keys_str_mv | AT lhumenatejano bioactivitiesofenzymaticproteinhydrolysatesderivedfromchlorellasorokiniana AT josepperalta bioactivitiesofenzymaticproteinhydrolysatesderivedfromchlorellasorokiniana AT encarnacionemiliasyap bioactivitiesofenzymaticproteinhydrolysatesderivedfromchlorellasorokiniana AT yuweichang bioactivitiesofenzymaticproteinhydrolysatesderivedfromchlorellasorokiniana |