Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities
Actinopyga lecanora (A. lecanora) is classified among the edible species of sea cucumber, known to be rich in protein. Its hydrolysates were reported to contain relatively high antioxidant activity. Antioxidants are one of the essential properties in cosmeceutical products especially to alleviate sk...
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| Format: | Article |
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MDPI
2020
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| Online Access: | http://psasir.upm.edu.my/id/eprint/87464/ |
| _version_ | 1848860443607564288 |
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| author | Bahari, Aqilah Noor Saari, Nazamid Salim, Norazlinaliza Ashari, Siti Efliza |
| author_facet | Bahari, Aqilah Noor Saari, Nazamid Salim, Norazlinaliza Ashari, Siti Efliza |
| author_sort | Bahari, Aqilah Noor |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Actinopyga lecanora (A. lecanora) is classified among the edible species of sea cucumber, known to be rich in protein. Its hydrolysates were reported to contain relatively high antioxidant activity. Antioxidants are one of the essential properties in cosmeceutical products especially to alleviate skin aging. In the present study, pH, reaction temperature, reaction time and enzyme/substrate ratio (E/S) have been identified as the parameters in the papain enzymatic hydrolysis of A. lecanora. The degree of hydrolysis (DH) with antioxidant activities of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric-reducing antioxidant power (FRAP) assays were used as the responses in the optimization. Analysis of variance (ANOVA), normal plot of residuals and 3D contour plots were evaluated to study the effects and interactions between parameters. The best conditions selected from the optimization were at pH 5.00, 70 °C of reaction temperature, 9 h of hydrolysis time and 1.00% enzyme/substrate (E/S) ratio, with the hydrolysates having 51.90% of DH, 42.70% of DPPH activity and 109.90 Fe2+μg/mL of FRAP activity. The A. lecanora hydrolysates (ALH) showed a high amount of hydrophobic amino acids (286.40 mg/g sample) that might be responsible for antioxidant and antityrosinase activities. Scanning electron microscopy (SEM) image of ALH shows smooth structures with pores. Antityrosinase activity of ALH exhibited inhibition of 31.50% for L-tyrosine substrate and 25.40% for L-DOPA substrate. This condition suggests that the optimized ALH acquired has the potential to be used as a bioactive ingredient for cosmeceutical applications. |
| first_indexed | 2025-11-15T12:45:19Z |
| format | Article |
| id | upm-87464 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T12:45:19Z |
| publishDate | 2020 |
| publisher | MDPI |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-874642023-05-30T02:27:02Z http://psasir.upm.edu.my/id/eprint/87464/ Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities Bahari, Aqilah Noor Saari, Nazamid Salim, Norazlinaliza Ashari, Siti Efliza Actinopyga lecanora (A. lecanora) is classified among the edible species of sea cucumber, known to be rich in protein. Its hydrolysates were reported to contain relatively high antioxidant activity. Antioxidants are one of the essential properties in cosmeceutical products especially to alleviate skin aging. In the present study, pH, reaction temperature, reaction time and enzyme/substrate ratio (E/S) have been identified as the parameters in the papain enzymatic hydrolysis of A. lecanora. The degree of hydrolysis (DH) with antioxidant activities of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric-reducing antioxidant power (FRAP) assays were used as the responses in the optimization. Analysis of variance (ANOVA), normal plot of residuals and 3D contour plots were evaluated to study the effects and interactions between parameters. The best conditions selected from the optimization were at pH 5.00, 70 °C of reaction temperature, 9 h of hydrolysis time and 1.00% enzyme/substrate (E/S) ratio, with the hydrolysates having 51.90% of DH, 42.70% of DPPH activity and 109.90 Fe2+μg/mL of FRAP activity. The A. lecanora hydrolysates (ALH) showed a high amount of hydrophobic amino acids (286.40 mg/g sample) that might be responsible for antioxidant and antityrosinase activities. Scanning electron microscopy (SEM) image of ALH shows smooth structures with pores. Antityrosinase activity of ALH exhibited inhibition of 31.50% for L-tyrosine substrate and 25.40% for L-DOPA substrate. This condition suggests that the optimized ALH acquired has the potential to be used as a bioactive ingredient for cosmeceutical applications. MDPI 2020-06 Article PeerReviewed Bahari, Aqilah Noor and Saari, Nazamid and Salim, Norazlinaliza and Ashari, Siti Efliza (2020) Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities. Molecules, 25 (11). art. no. 2663. pp. 1-21. ISSN 1420-3049 https://www.mdpi.com/1420-3049/25/11/2663 10.3390/molecules25112663 |
| spellingShingle | Bahari, Aqilah Noor Saari, Nazamid Salim, Norazlinaliza Ashari, Siti Efliza Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities |
| title | Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities |
| title_full | Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities |
| title_fullStr | Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities |
| title_full_unstemmed | Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities |
| title_short | Response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities |
| title_sort | response factorial design analysis on papaingenerated hydrolysates from actinopyga lecanora for determination of antioxidant and antityrosinase activities |
| url | http://psasir.upm.edu.my/id/eprint/87464/ http://psasir.upm.edu.my/id/eprint/87464/ http://psasir.upm.edu.my/id/eprint/87464/ |