| Autor: |
Arijit Nath, Abubakar Saleh Ahmad, Abraham Amankwaa, Barbara Csehi, Zsuzsanna Mednyánszky, Emőke Szerdahelyi, Attila Tóth, Judit Tormási, Duy Hoàng Truong, László Abrankó, András Koris |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Bioengineering, Vol 9, Iss 9, p 418 (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2306-5354 |
| DOI: |
10.3390/bioengineering9090418 |
| Popis: |
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−1, 0.016 g·L−1, 0.032 g·L−1 and 0.064 g·L−1). 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. |
| Databáze: |
Directory of Open Access Journals |
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