Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives
The objective of the investigation was to understand the biochemical activities of hydrolysate of soybean milk protein (SMP). Hydrolysis was carried out by different concentrations of papain (0.008 g·L<sup>−1</sup>, 0.016 g·L<sup>−1</sup>, 0.032 g·L<sup>−1</sup> a...
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MDPI AG
2022-08-01
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| Series: | Bioengineering |
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| Online Access: | https://www.mdpi.com/2306-5354/9/9/418 |
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| author | Arijit Nath Abubakar Saleh Ahmad Abraham Amankwaa Barbara Csehi Zsuzsanna Mednyánszky Emőke Szerdahelyi Attila Tóth Judit Tormási Duy Hoàng Truong László Abrankó András Koris |
| author_facet | Arijit Nath Abubakar Saleh Ahmad Abraham Amankwaa Barbara Csehi Zsuzsanna Mednyánszky Emőke Szerdahelyi Attila Tóth Judit Tormási Duy Hoàng Truong László Abrankó András Koris |
| author_sort | Arijit Nath |
| collection | DOAJ |
| description | The objective of the investigation was to understand the biochemical activities of hydrolysate of soybean milk protein (SMP). Hydrolysis was carried out by different concentrations of papain (0.008 g·L<sup>−1</sup>, 0.016 g·L<sup>−1</sup>, 0.032 g·L<sup>−1</sup> and 0.064 g·L<sup>−1</sup>). The antioxidant capacity was measured by the ferric-reducing ability of plasma (FRAP) and 2,2-Diphenyl-1-picrylhydrazyl (DPPH) assays. The anti-angiotensin activity of hydrolysate was measured by the recombinant angiotensin converting enzyme and substrate Abz-FRK(Dnp)-P. The contributions of the Kunitz trypsin inhibitor (KTI) and Bowman–Birk inhibitor (BBI) on antigenicity, and the in vitro digestion of papain-hydrolyzed SMP were studied. Rabbit polyclonal anti-KTI and anti-BBI antibodies together with peroxidase-labelled goat anti-Rb IgG secondary antibody were used to identify the antigenicity of KTI and BBI in unhydrolyzed and papain-hydrolyzed SMP. The antioxidant capacity and anti-angiotensin activity of SMP were increased after the papain hydrolysis of SMP. The KTI- and BBI-specific antigenicity were reduced in SMP by increasing the concentration of papain. However, there was interaction between papain-hydrolyzed SMP and trypsin in native gel, while interaction with chymotrypsin was absent. The interaction between trypsin and SMP was reduced due to the hydrolysis of papain in a concentration-dependent manner. According to the in vitro gastrointestinal digestion simulation protocol (Infogest), the digestibility of SMP was not statistically increased. |
| first_indexed | 2024-03-10T00:42:45Z |
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| id | doaj.art-f7648b8877e649f1a9652fd495dde575 |
| institution | Directory Open Access Journal |
| issn | 2306-5354 |
| language | English |
| last_indexed | 2024-03-10T00:42:45Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Bioengineering |
| spelling | doaj.art-f7648b8877e649f1a9652fd495dde5752023-11-23T15:05:17ZengMDPI AGBioengineering2306-53542022-08-019941810.3390/bioengineering9090418Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility PerspectivesArijit Nath0Abubakar Saleh Ahmad1Abraham Amankwaa2Barbara Csehi3Zsuzsanna Mednyánszky4Emőke Szerdahelyi5Attila Tóth6Judit Tormási7Duy Hoàng Truong8László Abrankó9András Koris10Department of Food Process Engineering, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi St 44, HU-1118 Budapest, HungaryDepartment of Food Process Engineering, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi St 44, HU-1118 Budapest, HungaryDepartment of Food Process Engineering, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi St 44, HU-1118 Budapest, HungaryDepartment of Refrigeration and Livestock Products Technology, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi út 43-45, HU-1118 Budapest, HungaryDepartment of Nutrition, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Somlói St 14-16, HU-1118 Budapest, HungaryDepartment of Nutrition, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Somlói St 14-16, HU-1118 Budapest, HungaryDivision of Clinical Physiology, Department of Cardiology, Faculty of Medicine, University of Debrecen, Móricz Zsigmond Str 22, HU-4032 Debrecen, HungaryDepartment of Food Chemistry and Analytical Chemistry, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Villányi út 35-43, HU-1118 Budapest, HungaryInstitute of Biotechnology and Food Technology, Industrial University of Ho Chi Minh City, 12 Nguyen Van Bao, Ward 4, Go Vap District, Ho Chi Minh City 727000, VietnamDepartment of Food Chemistry and Analytical Chemistry, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Villányi út 35-43, HU-1118 Budapest, HungaryDepartment of Food Process Engineering, Institute of Food Science and Technology, Hungarian University of Agriculture and Life Sciences, Ménesi St 44, HU-1118 Budapest, HungaryThe objective of the investigation was to understand the biochemical activities of hydrolysate of soybean milk protein (SMP). Hydrolysis was carried out by different concentrations of papain (0.008 g·L<sup>−1</sup>, 0.016 g·L<sup>−1</sup>, 0.032 g·L<sup>−1</sup> and 0.064 g·L<sup>−1</sup>). The antioxidant capacity was measured by the ferric-reducing ability of plasma (FRAP) and 2,2-Diphenyl-1-picrylhydrazyl (DPPH) assays. The anti-angiotensin activity of hydrolysate was measured by the recombinant angiotensin converting enzyme and substrate Abz-FRK(Dnp)-P. The contributions of the Kunitz trypsin inhibitor (KTI) and Bowman–Birk inhibitor (BBI) on antigenicity, and the in vitro digestion of papain-hydrolyzed SMP were studied. Rabbit polyclonal anti-KTI and anti-BBI antibodies together with peroxidase-labelled goat anti-Rb IgG secondary antibody were used to identify the antigenicity of KTI and BBI in unhydrolyzed and papain-hydrolyzed SMP. The antioxidant capacity and anti-angiotensin activity of SMP were increased after the papain hydrolysis of SMP. The KTI- and BBI-specific antigenicity were reduced in SMP by increasing the concentration of papain. However, there was interaction between papain-hydrolyzed SMP and trypsin in native gel, while interaction with chymotrypsin was absent. The interaction between trypsin and SMP was reduced due to the hydrolysis of papain in a concentration-dependent manner. According to the in vitro gastrointestinal digestion simulation protocol (Infogest), the digestibility of SMP was not statistically increased.https://www.mdpi.com/2306-5354/9/9/418soybean milk proteinantioxidant capacityanti-angiotensin activityantigenic propertydigestibility |
| spellingShingle | Arijit Nath Abubakar Saleh Ahmad Abraham Amankwaa Barbara Csehi Zsuzsanna Mednyánszky Emőke Szerdahelyi Attila Tóth Judit Tormási Duy Hoàng Truong László Abrankó András Koris Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives Bioengineering soybean milk protein antioxidant capacity anti-angiotensin activity antigenic property digestibility |
| title | Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives |
| title_full | Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives |
| title_fullStr | Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives |
| title_full_unstemmed | Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives |
| title_short | Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives |
| title_sort | hydrolysis of soybean milk protein by papain antioxidant anti angiotensin antigenic and digestibility perspectives |
| topic | soybean milk protein antioxidant capacity anti-angiotensin activity antigenic property digestibility |
| url | https://www.mdpi.com/2306-5354/9/9/418 |
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