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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Autor*in:	Chengwei Yu [verfasserIn] Bin Peng [verfasserIn] Ting Luo [verfasserIn] Zeyuan Deng [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	Rice bran Bound lipase Pectin Catalytic activity

Übergeordnetes Werk:	In: Food Science and Human Wellness - KeAi Communications Co., Ltd., 2016, 12(2023), 5, Seite 1779-1787
Übergeordnetes Werk:	volume:12 ; year:2023 ; number:5 ; pages:1779-1787

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.fshw.2023.02.030

Katalog-ID:	DOAJ087663120

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spelling	10.1016/j.fshw.2023.02.030 doi (DE-627)DOAJ087663120 (DE-599)DOAJcaf8f681594b421f9928dba597ec3bb0 DE-627 ger DE-627 rakwb eng TX341-641 Chengwei Yu verfasserin aut Bound lipase: an important form of lipase in rice bran (Oryza sativa) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. Rice bran Bound lipase Pectin Catalytic activity Nutrition. Foods and food supply Bin Peng verfasserin aut Ting Luo verfasserin aut Zeyuan Deng verfasserin aut In Food Science and Human Wellness KeAi Communications Co., Ltd., 2016 12(2023), 5, Seite 1779-1787 (DE-627)742744027 (DE-600)2712869-6 22134530 nnns volume:12 year:2023 number:5 pages:1779-1787 https://doi.org/10.1016/j.fshw.2023.02.030 kostenfrei https://doaj.org/article/caf8f681594b421f9928dba597ec3bb0 kostenfrei http://www.sciencedirect.com/science/article/pii/S2213453023000307 kostenfrei https://doaj.org/toc/2213-4530 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 12 2023 5 1779-1787
allfields_unstemmed	10.1016/j.fshw.2023.02.030 doi (DE-627)DOAJ087663120 (DE-599)DOAJcaf8f681594b421f9928dba597ec3bb0 DE-627 ger DE-627 rakwb eng TX341-641 Chengwei Yu verfasserin aut Bound lipase: an important form of lipase in rice bran (Oryza sativa) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. Rice bran Bound lipase Pectin Catalytic activity Nutrition. Foods and food supply Bin Peng verfasserin aut Ting Luo verfasserin aut Zeyuan Deng verfasserin aut In Food Science and Human Wellness KeAi Communications Co., Ltd., 2016 12(2023), 5, Seite 1779-1787 (DE-627)742744027 (DE-600)2712869-6 22134530 nnns volume:12 year:2023 number:5 pages:1779-1787 https://doi.org/10.1016/j.fshw.2023.02.030 kostenfrei https://doaj.org/article/caf8f681594b421f9928dba597ec3bb0 kostenfrei http://www.sciencedirect.com/science/article/pii/S2213453023000307 kostenfrei https://doaj.org/toc/2213-4530 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 12 2023 5 1779-1787
allfieldsGer	10.1016/j.fshw.2023.02.030 doi (DE-627)DOAJ087663120 (DE-599)DOAJcaf8f681594b421f9928dba597ec3bb0 DE-627 ger DE-627 rakwb eng TX341-641 Chengwei Yu verfasserin aut Bound lipase: an important form of lipase in rice bran (Oryza sativa) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. Rice bran Bound lipase Pectin Catalytic activity Nutrition. Foods and food supply Bin Peng verfasserin aut Ting Luo verfasserin aut Zeyuan Deng verfasserin aut In Food Science and Human Wellness KeAi Communications Co., Ltd., 2016 12(2023), 5, Seite 1779-1787 (DE-627)742744027 (DE-600)2712869-6 22134530 nnns volume:12 year:2023 number:5 pages:1779-1787 https://doi.org/10.1016/j.fshw.2023.02.030 kostenfrei https://doaj.org/article/caf8f681594b421f9928dba597ec3bb0 kostenfrei http://www.sciencedirect.com/science/article/pii/S2213453023000307 kostenfrei https://doaj.org/toc/2213-4530 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 12 2023 5 1779-1787
allfieldsSound	10.1016/j.fshw.2023.02.030 doi (DE-627)DOAJ087663120 (DE-599)DOAJcaf8f681594b421f9928dba597ec3bb0 DE-627 ger DE-627 rakwb eng TX341-641 Chengwei Yu verfasserin aut Bound lipase: an important form of lipase in rice bran (Oryza sativa) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. Rice bran Bound lipase Pectin Catalytic activity Nutrition. Foods and food supply Bin Peng verfasserin aut Ting Luo verfasserin aut Zeyuan Deng verfasserin aut In Food Science and Human Wellness KeAi Communications Co., Ltd., 2016 12(2023), 5, Seite 1779-1787 (DE-627)742744027 (DE-600)2712869-6 22134530 nnns volume:12 year:2023 number:5 pages:1779-1787 https://doi.org/10.1016/j.fshw.2023.02.030 kostenfrei https://doaj.org/article/caf8f681594b421f9928dba597ec3bb0 kostenfrei http://www.sciencedirect.com/science/article/pii/S2213453023000307 kostenfrei https://doaj.org/toc/2213-4530 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4367 GBV_ILN_4700 AR 12 2023 5 1779-1787
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callnumber-first	T - Technology
author	Chengwei Yu
spellingShingle	Chengwei Yu misc TX341-641 misc Rice bran misc Bound lipase misc Pectin misc Catalytic activity misc Nutrition. Foods and food supply Bound lipase: an important form of lipase in rice bran (Oryza sativa)
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topic_title	TX341-641 Bound lipase: an important form of lipase in rice bran (Oryza sativa) Rice bran Bound lipase Pectin Catalytic activity
topic	misc TX341-641 misc Rice bran misc Bound lipase misc Pectin misc Catalytic activity misc Nutrition. Foods and food supply
topic_unstemmed	misc TX341-641 misc Rice bran misc Bound lipase misc Pectin misc Catalytic activity misc Nutrition. Foods and food supply
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title	Bound lipase: an important form of lipase in rice bran (Oryza sativa)
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title_full	Bound lipase: an important form of lipase in rice bran (Oryza sativa)
author_sort	Chengwei Yu
journal	Food Science and Human Wellness
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author_browse	Chengwei Yu Bin Peng Ting Luo Zeyuan Deng
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doi_str_mv	10.1016/j.fshw.2023.02.030
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title_sort	bound lipase: an important form of lipase in rice bran (oryza sativa)
callnumber	TX341-641
title_auth	Bound lipase: an important form of lipase in rice bran (Oryza sativa)
abstract	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.
abstractGer	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.
abstract_unstemmed	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.
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title_short	Bound lipase: an important form of lipase in rice bran (Oryza sativa)
url	https://doi.org/10.1016/j.fshw.2023.02.030 https://doaj.org/article/caf8f681594b421f9928dba597ec3bb0 http://www.sciencedirect.com/science/article/pii/S2213453023000307 https://doaj.org/toc/2213-4530
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Bound lipase: an important form of lipase in rice bran (Oryza sativa)

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Vorhandene Bände

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