Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity

The enzymatic hydrolysis of palm kernel cake protein (PKCP) with trypsin to obtain PKCP hydrolysates (PKCPH) was optimized using response surface methodology (RSM). A central composite design (CCD) was used to study the influence of four independent variables, namely pH, hydrolysis temperature (°C),...

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Main Authors: Ng, Khar Ling, Ayob, Mohd Khan, Said, Mamot, Osman, Md. Anuar, Ismail, Amin
Format: Article
Language:English
Published: Elsevier 2013
Online Access:http://psasir.upm.edu.my/id/eprint/29773/1/Optimization%20of%20enzymatic%20hydrolysis%20of%20palm%20kernel%20cake%20protein.pdf
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author Ng, Khar Ling
Ayob, Mohd Khan
Said, Mamot
Osman, Md. Anuar
Ismail, Amin
author_facet Ng, Khar Ling
Ayob, Mohd Khan
Said, Mamot
Osman, Md. Anuar
Ismail, Amin
author_sort Ng, Khar Ling
collection UPM
description The enzymatic hydrolysis of palm kernel cake protein (PKCP) with trypsin to obtain PKCP hydrolysates (PKCPH) was optimized using response surface methodology (RSM). A central composite design (CCD) was used to study the influence of four independent variables, namely pH, hydrolysis temperature (°C), substrate concentration (w/v) and enzyme/substrate (w/w) ratio on the degree of hydrolysis (DH%). The hydrolysis was carried out using different combinations of four hydrolytic parameters at five levels for 6h. The CCD consisted of 24 experimental points and six replicates of the central points. The data were analyzed using Design-Expert Software. The results showed that all of the variables evaluated significantly influenced the DH% in a second polynomial model, and different combinations of parameters were generated to obtain three different levels of DH (30%, 40% and 50%), namely PKCPH 30, PKCPH 40 and PKCPH 50. The PKCPH with different DH% showed significantly different antiradical properties (p<0.05). The PKCPH 50 preparation had the lowest EC 50 value for DPPH radical scavenging capacity (0.14mg/ml). In the ABTS + radical scavenging capacity and PCL-ACW (photo chemiluminescence-antiradical capacity of water soluble substances) assays, PKCPH 50 showed the highest Trolox equivalent antioxidant capacity value (326.67±5.77μmol TEAC/g) and ascorbic acid equivalent value (11.43±0.03μg AAE/mg) of the preparations tested. Moreover, the protein hydrolysates also exhibited a notable reducing effect in a dose-dependent manner. Optimum conditions for enzymatic hydrolysis of PKCP were established in this study to produce an antiradical agent.
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spelling upm.eprints-297732015-12-07T03:53:50Z http://psasir.upm.edu.my/id/eprint/29773/ Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity Ng, Khar Ling Ayob, Mohd Khan Said, Mamot Osman, Md. Anuar Ismail, Amin The enzymatic hydrolysis of palm kernel cake protein (PKCP) with trypsin to obtain PKCP hydrolysates (PKCPH) was optimized using response surface methodology (RSM). A central composite design (CCD) was used to study the influence of four independent variables, namely pH, hydrolysis temperature (°C), substrate concentration (w/v) and enzyme/substrate (w/w) ratio on the degree of hydrolysis (DH%). The hydrolysis was carried out using different combinations of four hydrolytic parameters at five levels for 6h. The CCD consisted of 24 experimental points and six replicates of the central points. The data were analyzed using Design-Expert Software. The results showed that all of the variables evaluated significantly influenced the DH% in a second polynomial model, and different combinations of parameters were generated to obtain three different levels of DH (30%, 40% and 50%), namely PKCPH 30, PKCPH 40 and PKCPH 50. The PKCPH with different DH% showed significantly different antiradical properties (p<0.05). The PKCPH 50 preparation had the lowest EC 50 value for DPPH radical scavenging capacity (0.14mg/ml). In the ABTS + radical scavenging capacity and PCL-ACW (photo chemiluminescence-antiradical capacity of water soluble substances) assays, PKCPH 50 showed the highest Trolox equivalent antioxidant capacity value (326.67±5.77μmol TEAC/g) and ascorbic acid equivalent value (11.43±0.03μg AAE/mg) of the preparations tested. Moreover, the protein hydrolysates also exhibited a notable reducing effect in a dose-dependent manner. Optimum conditions for enzymatic hydrolysis of PKCP were established in this study to produce an antiradical agent. Elsevier 2013-05 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/29773/1/Optimization%20of%20enzymatic%20hydrolysis%20of%20palm%20kernel%20cake%20protein.pdf Ng, Khar Ling and Ayob, Mohd Khan and Said, Mamot and Osman, Md. Anuar and Ismail, Amin (2013) Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity. Industrial Crops and Products, 43 (1). pp. 725-731. ISSN 0926-6690 10.1016/j.indcrop.2012.08.017
spellingShingle Ng, Khar Ling
Ayob, Mohd Khan
Said, Mamot
Osman, Md. Anuar
Ismail, Amin
Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity
title Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity
title_full Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity
title_fullStr Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity
title_full_unstemmed Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity
title_short Optimization of enzymatic hydrolysis of palm kernel cake protein (PKCP) for producing hydrolysates with antiradical capacity
title_sort optimization of enzymatic hydrolysis of palm kernel cake protein pkcp for producing hydrolysates with antiradical capacity
url http://psasir.upm.edu.my/id/eprint/29773/1/Optimization%20of%20enzymatic%20hydrolysis%20of%20palm%20kernel%20cake%20protein.pdf
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