Bound lipase: an important form of lipase in rice bran (Oryza sativa)
Rice bran residue possessed a steady lipase activity ((26.68 ± 3.69)%) after its endogenous lipase was extracted continuously by phosphate buffer solution (PBS) for 24 h. Therefore, the aim of this research was to explore whether there exist any bound lipases in rice bran (Oryza sativa). Three physi...
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Tsinghua University Press
2023-09-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453023000307 |
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| author | Chengwei Yu Bin Peng Ting Luo Zeyuan Deng |
| author_facet | Chengwei Yu Bin Peng Ting Luo Zeyuan Deng |
| author_sort | Chengwei Yu |
| collection | DOAJ |
| description | Rice bran residue possessed a steady lipase activity ((26.68 ± 3.69)%) after its endogenous lipase was extracted continuously by phosphate buffer solution (PBS) for 24 h. Therefore, the aim of this research was to explore whether there exist any bound lipases in rice bran (Oryza sativa). Three physical treatments (grinding, homogenizing and ultrasound crush) and 6 enzymatic treatments (cellulase, hemicellulase, pectinase, complex cellulase, glucoamylase and α-amylase) were applied to rice bran in order to investigate this bound lipase. The relative catalytic activities of extraction supernatant and residue for pectinase group were (437.63 ± 22.54)% and (159.26 ± 2.12)%, respectively, which were significantly higher (P < 0.05) than other groups. This phenomenon demonstrated that lipase was the most likely to combine with pectin. Molecular simulation proved that pectin could combine with two rice bran lipases (lipase 315 and lipase 308) and cover the catalytic centers so as to prevent the lipases from encountering the substrate and inhibiting their catalytic activities. During combination, pectin could make the lipases more compact and reduce the solvent accessible surface area of lipases, which would make the lipases inactive to molecular interaction. In summary, part of rice bran lipase was proved to exist in bound form and combined with the pectin. |
| format | Article |
| id | doaj-art-caf8f681594b421f9928dba597ec3bb0 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2023-09-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-caf8f681594b421f9928dba597ec3bb02025-02-03T00:27:37ZengTsinghua University PressFood Science and Human Wellness2213-45302023-09-0112517791787Bound lipase: an important form of lipase in rice bran (Oryza sativa)Chengwei Yu0Bin Peng1Ting Luo2Zeyuan Deng3State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; School of Health, Jiangxi Normal University, Nanchang 330022, China; Department of Food Science and Technology, National University of Singapore, Singapore 117542, Singapore; National Research and Development Center of Freshwater Fish Processing, Jiangxi Normal University, Nanchang 330022, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; National Research and Development Center of Freshwater Fish Processing, Jiangxi Normal University, Nanchang 330022, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, ChinaState Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; Corresponding author at: State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047. China.Rice bran residue possessed a steady lipase activity ((26.68 ± 3.69)%) after its endogenous lipase was extracted continuously by phosphate buffer solution (PBS) for 24 h. Therefore, the aim of this research was to explore whether there exist any bound lipases in rice bran (Oryza sativa). Three physical treatments (grinding, homogenizing and ultrasound crush) and 6 enzymatic treatments (cellulase, hemicellulase, pectinase, complex cellulase, glucoamylase and α-amylase) were applied to rice bran in order to investigate this bound lipase. The relative catalytic activities of extraction supernatant and residue for pectinase group were (437.63 ± 22.54)% and (159.26 ± 2.12)%, respectively, which were significantly higher (P < 0.05) than other groups. This phenomenon demonstrated that lipase was the most likely to combine with pectin. Molecular simulation proved that pectin could combine with two rice bran lipases (lipase 315 and lipase 308) and cover the catalytic centers so as to prevent the lipases from encountering the substrate and inhibiting their catalytic activities. During combination, pectin could make the lipases more compact and reduce the solvent accessible surface area of lipases, which would make the lipases inactive to molecular interaction. In summary, part of rice bran lipase was proved to exist in bound form and combined with the pectin.http://www.sciencedirect.com/science/article/pii/S2213453023000307Rice branBound lipasePectinCatalytic activity |
| spellingShingle | Chengwei Yu Bin Peng Ting Luo Zeyuan Deng Bound lipase: an important form of lipase in rice bran (Oryza sativa) Food Science and Human Wellness Rice bran Bound lipase Pectin Catalytic activity |
| title | Bound lipase: an important form of lipase in rice bran (Oryza sativa) |
| title_full | Bound lipase: an important form of lipase in rice bran (Oryza sativa) |
| title_fullStr | Bound lipase: an important form of lipase in rice bran (Oryza sativa) |
| title_full_unstemmed | Bound lipase: an important form of lipase in rice bran (Oryza sativa) |
| title_short | Bound lipase: an important form of lipase in rice bran (Oryza sativa) |
| title_sort | bound lipase an important form of lipase in rice bran oryza sativa |
| topic | Rice bran Bound lipase Pectin Catalytic activity |
| url | http://www.sciencedirect.com/science/article/pii/S2213453023000307 |
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