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An in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran
De-oiled rice bran (DORB) is a potentially useful by-product of the rice bran oil industry. DORB may prove to be an important protein source, and also contains many other micronutrients. This study has the principal aim of optimizing the process of DORB protein hydrolysate preparation, and then test...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9033478/ https://www.ncbi.nlm.nih.gov/pubmed/35478653 http://dx.doi.org/10.1039/d1ra01411k |
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author | Ketprayoon, Titima Noitang, Sajee Sangtanoo, Papassara Srimongkol, Piroonporn Saisavoey, Tanatorn Reamtong, Onrapak Choowongkomon, Kiattawee Karnchanatat, Aphichart |
author_facet | Ketprayoon, Titima Noitang, Sajee Sangtanoo, Papassara Srimongkol, Piroonporn Saisavoey, Tanatorn Reamtong, Onrapak Choowongkomon, Kiattawee Karnchanatat, Aphichart |
author_sort | Ketprayoon, Titima |
collection | PubMed |
description | De-oiled rice bran (DORB) is a potentially useful by-product of the rice bran oil industry. DORB may prove to be an important protein source, and also contains many other micronutrients. This study has the principal aim of optimizing the process of DORB protein hydrolysate preparation, and then testing the hydrolysate to determine its lipase inhibitory activity. DORB underwent hydrolysis using Alcalase® and response surface methodology (RSM). The resulting degree of hydrolysis (DH) was then monitored along with the extent of any lipase inhibitory activity. The optimum levels of lipase inhibition were obtained at a temperature of 49.88 °C, a duration of 150.43 minutes, and 1.53% Alcalase® used for the sample 5% (w/v) solution. In these conditions, the DH value was 35.65%, and the IC(50) value for lipase inhibitory activity was 2.84 μg mL(−1). Five ranges of different molecular weights were obtained via fractionation, whereupon it was determined that the highest level of inhibitory activity was achieved by the <0.65 kDa fraction. This fraction was then further purified via RP-HPLC, and the resulting peak had a retention time of 21.75 minutes (F(2) sub-fraction) and exhibited high lipase inhibitory activity. Mass spectrometry was used to determine the amino acid sequence for this peak, identified as FYLGYCDY. This particular peptide is categorized as bitter, with a non-toxic profile, and having poor water solubility. The synthesized form of this peptide showed lipase inhibitory activity measured by an IC(50) value of 0.47 ± 0.02 μM. The Lineweaver–Burk plot revealed that FYLGYCDY is a non-competitive inhibitor, while analysis of the docking results provided details of the FYLGYCDY peptide binding site with the porcine pancreatic lipase (PPL) complex, which is a competitive type. It can be inferred from these findings that DORB may prove a useful raw material source for the production of anti-obesity peptides which might enhance the therapeutic and commercial performance of functional foods and healthcare products. |
format | Online Article Text |
id | pubmed-9033478 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-90334782022-04-26 An in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran Ketprayoon, Titima Noitang, Sajee Sangtanoo, Papassara Srimongkol, Piroonporn Saisavoey, Tanatorn Reamtong, Onrapak Choowongkomon, Kiattawee Karnchanatat, Aphichart RSC Adv Chemistry De-oiled rice bran (DORB) is a potentially useful by-product of the rice bran oil industry. DORB may prove to be an important protein source, and also contains many other micronutrients. This study has the principal aim of optimizing the process of DORB protein hydrolysate preparation, and then testing the hydrolysate to determine its lipase inhibitory activity. DORB underwent hydrolysis using Alcalase® and response surface methodology (RSM). The resulting degree of hydrolysis (DH) was then monitored along with the extent of any lipase inhibitory activity. The optimum levels of lipase inhibition were obtained at a temperature of 49.88 °C, a duration of 150.43 minutes, and 1.53% Alcalase® used for the sample 5% (w/v) solution. In these conditions, the DH value was 35.65%, and the IC(50) value for lipase inhibitory activity was 2.84 μg mL(−1). Five ranges of different molecular weights were obtained via fractionation, whereupon it was determined that the highest level of inhibitory activity was achieved by the <0.65 kDa fraction. This fraction was then further purified via RP-HPLC, and the resulting peak had a retention time of 21.75 minutes (F(2) sub-fraction) and exhibited high lipase inhibitory activity. Mass spectrometry was used to determine the amino acid sequence for this peak, identified as FYLGYCDY. This particular peptide is categorized as bitter, with a non-toxic profile, and having poor water solubility. The synthesized form of this peptide showed lipase inhibitory activity measured by an IC(50) value of 0.47 ± 0.02 μM. The Lineweaver–Burk plot revealed that FYLGYCDY is a non-competitive inhibitor, while analysis of the docking results provided details of the FYLGYCDY peptide binding site with the porcine pancreatic lipase (PPL) complex, which is a competitive type. It can be inferred from these findings that DORB may prove a useful raw material source for the production of anti-obesity peptides which might enhance the therapeutic and commercial performance of functional foods and healthcare products. The Royal Society of Chemistry 2021-05-25 /pmc/articles/PMC9033478/ /pubmed/35478653 http://dx.doi.org/10.1039/d1ra01411k Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/ |
spellingShingle | Chemistry Ketprayoon, Titima Noitang, Sajee Sangtanoo, Papassara Srimongkol, Piroonporn Saisavoey, Tanatorn Reamtong, Onrapak Choowongkomon, Kiattawee Karnchanatat, Aphichart An in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran |
title | An in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran |
title_full | An in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran |
title_fullStr | An in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran |
title_full_unstemmed | An in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran |
title_short | An in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran |
title_sort | in vitro study of lipase inhibitory peptides obtained from de-oiled rice bran |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9033478/ https://www.ncbi.nlm.nih.gov/pubmed/35478653 http://dx.doi.org/10.1039/d1ra01411k |
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