Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino)

Polyphenol oxidase (PPO) in plants plays an important role in browning reactions and may affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitat...
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Autor*in:	Siyu Liu [verfasserIn] Ayesha Murtaza [verfasserIn] Yan Liu [verfasserIn] Wanfeng Hu [verfasserIn] Xiaoyun Xu [verfasserIn] Siyi Pan [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2018

Schlagwörter:	browning-related protein (BRP) polyphenol oxidase (PPO) purification melon structural characterization

Übergeordnetes Werk:	In: Frontiers in Chemistry - Frontiers Media S.A., 2014, 6(2018)
Übergeordnetes Werk:	volume:6 ; year:2018

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fchem.2018.00354

Katalog-ID:	DOAJ001127608

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spelling	10.3389/fchem.2018.00354 doi (DE-627)DOAJ001127608 (DE-599)DOAJb94ad81dea274e1dbad61e786a16f9f8 DE-627 ger DE-627 rakwb eng QD1-999 Siyu Liu verfasserin aut Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino) 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidase (PPO) in plants plays an important role in browning reactions and may affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitation and column chromatography. The BRP possessed a high degree of identity with several chitinase proteins, particularly defense-related proteins, by MS identification. Pyrogallol was determined as the most appropriate substrate for BRP (Km = 0.04278 M). BRP exhibited extreme resistance under alkaline and high temperature conditions when pyrogallol was used as substrate. Polyacrylamide gel electrophoresis (PAGE) analysis indicated that BRP was a homo-dimer of two subunits and had a molecular weight of 37 kDa. Structural analysis indicated that the α-helix was the dominant conformation of BRP. The active site of the protein might be buried deeply in the protein, and BRP might be monodispersed in an aqueous system. browning-related protein (BRP) polyphenol oxidase (PPO) purification melon structural characterization Chemistry Ayesha Murtaza verfasserin aut Ayesha Murtaza verfasserin aut Yan Liu verfasserin aut Wanfeng Hu verfasserin aut Wanfeng Hu verfasserin aut Xiaoyun Xu verfasserin aut Xiaoyun Xu verfasserin aut Siyi Pan verfasserin aut Siyi Pan verfasserin aut In Frontiers in Chemistry Frontiers Media S.A., 2014 6(2018) (DE-627)742224538 (DE-600)2711776-5 22962646 nnns volume:6 year:2018 https://doi.org/10.3389/fchem.2018.00354 kostenfrei https://doaj.org/article/b94ad81dea274e1dbad61e786a16f9f8 kostenfrei https://www.frontiersin.org/article/10.3389/fchem.2018.00354/full kostenfrei https://doaj.org/toc/2296-2646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2018
allfields_unstemmed	10.3389/fchem.2018.00354 doi (DE-627)DOAJ001127608 (DE-599)DOAJb94ad81dea274e1dbad61e786a16f9f8 DE-627 ger DE-627 rakwb eng QD1-999 Siyu Liu verfasserin aut Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino) 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidase (PPO) in plants plays an important role in browning reactions and may affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitation and column chromatography. The BRP possessed a high degree of identity with several chitinase proteins, particularly defense-related proteins, by MS identification. Pyrogallol was determined as the most appropriate substrate for BRP (Km = 0.04278 M). BRP exhibited extreme resistance under alkaline and high temperature conditions when pyrogallol was used as substrate. Polyacrylamide gel electrophoresis (PAGE) analysis indicated that BRP was a homo-dimer of two subunits and had a molecular weight of 37 kDa. Structural analysis indicated that the α-helix was the dominant conformation of BRP. The active site of the protein might be buried deeply in the protein, and BRP might be monodispersed in an aqueous system. browning-related protein (BRP) polyphenol oxidase (PPO) purification melon structural characterization Chemistry Ayesha Murtaza verfasserin aut Ayesha Murtaza verfasserin aut Yan Liu verfasserin aut Wanfeng Hu verfasserin aut Wanfeng Hu verfasserin aut Xiaoyun Xu verfasserin aut Xiaoyun Xu verfasserin aut Siyi Pan verfasserin aut Siyi Pan verfasserin aut In Frontiers in Chemistry Frontiers Media S.A., 2014 6(2018) (DE-627)742224538 (DE-600)2711776-5 22962646 nnns volume:6 year:2018 https://doi.org/10.3389/fchem.2018.00354 kostenfrei https://doaj.org/article/b94ad81dea274e1dbad61e786a16f9f8 kostenfrei https://www.frontiersin.org/article/10.3389/fchem.2018.00354/full kostenfrei https://doaj.org/toc/2296-2646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2018
allfieldsGer	10.3389/fchem.2018.00354 doi (DE-627)DOAJ001127608 (DE-599)DOAJb94ad81dea274e1dbad61e786a16f9f8 DE-627 ger DE-627 rakwb eng QD1-999 Siyu Liu verfasserin aut Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino) 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidase (PPO) in plants plays an important role in browning reactions and may affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitation and column chromatography. The BRP possessed a high degree of identity with several chitinase proteins, particularly defense-related proteins, by MS identification. Pyrogallol was determined as the most appropriate substrate for BRP (Km = 0.04278 M). BRP exhibited extreme resistance under alkaline and high temperature conditions when pyrogallol was used as substrate. Polyacrylamide gel electrophoresis (PAGE) analysis indicated that BRP was a homo-dimer of two subunits and had a molecular weight of 37 kDa. Structural analysis indicated that the α-helix was the dominant conformation of BRP. The active site of the protein might be buried deeply in the protein, and BRP might be monodispersed in an aqueous system. browning-related protein (BRP) polyphenol oxidase (PPO) purification melon structural characterization Chemistry Ayesha Murtaza verfasserin aut Ayesha Murtaza verfasserin aut Yan Liu verfasserin aut Wanfeng Hu verfasserin aut Wanfeng Hu verfasserin aut Xiaoyun Xu verfasserin aut Xiaoyun Xu verfasserin aut Siyi Pan verfasserin aut Siyi Pan verfasserin aut In Frontiers in Chemistry Frontiers Media S.A., 2014 6(2018) (DE-627)742224538 (DE-600)2711776-5 22962646 nnns volume:6 year:2018 https://doi.org/10.3389/fchem.2018.00354 kostenfrei https://doaj.org/article/b94ad81dea274e1dbad61e786a16f9f8 kostenfrei https://www.frontiersin.org/article/10.3389/fchem.2018.00354/full kostenfrei https://doaj.org/toc/2296-2646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2018
allfieldsSound	10.3389/fchem.2018.00354 doi (DE-627)DOAJ001127608 (DE-599)DOAJb94ad81dea274e1dbad61e786a16f9f8 DE-627 ger DE-627 rakwb eng QD1-999 Siyu Liu verfasserin aut Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino) 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidase (PPO) in plants plays an important role in browning reactions and may affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitation and column chromatography. The BRP possessed a high degree of identity with several chitinase proteins, particularly defense-related proteins, by MS identification. Pyrogallol was determined as the most appropriate substrate for BRP (Km = 0.04278 M). BRP exhibited extreme resistance under alkaline and high temperature conditions when pyrogallol was used as substrate. Polyacrylamide gel electrophoresis (PAGE) analysis indicated that BRP was a homo-dimer of two subunits and had a molecular weight of 37 kDa. Structural analysis indicated that the α-helix was the dominant conformation of BRP. The active site of the protein might be buried deeply in the protein, and BRP might be monodispersed in an aqueous system. browning-related protein (BRP) polyphenol oxidase (PPO) purification melon structural characterization Chemistry Ayesha Murtaza verfasserin aut Ayesha Murtaza verfasserin aut Yan Liu verfasserin aut Wanfeng Hu verfasserin aut Wanfeng Hu verfasserin aut Xiaoyun Xu verfasserin aut Xiaoyun Xu verfasserin aut Siyi Pan verfasserin aut Siyi Pan verfasserin aut In Frontiers in Chemistry Frontiers Media S.A., 2014 6(2018) (DE-627)742224538 (DE-600)2711776-5 22962646 nnns volume:6 year:2018 https://doi.org/10.3389/fchem.2018.00354 kostenfrei https://doaj.org/article/b94ad81dea274e1dbad61e786a16f9f8 kostenfrei https://www.frontiersin.org/article/10.3389/fchem.2018.00354/full kostenfrei https://doaj.org/toc/2296-2646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2018
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authorswithroles_txt_mv	Siyu Liu @@aut@@ Ayesha Murtaza @@aut@@ Yan Liu @@aut@@ Wanfeng Hu @@aut@@ Xiaoyun Xu @@aut@@ Siyi Pan @@aut@@
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callnumber-first	Q - Science
author	Siyu Liu
spellingShingle	Siyu Liu misc QD1-999 misc browning-related protein (BRP) misc polyphenol oxidase (PPO) misc purification misc melon misc structural characterization misc Chemistry Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino)
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topic_title	QD1-999 Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino) browning-related protein (BRP) polyphenol oxidase (PPO) purification melon structural characterization
topic	misc QD1-999 misc browning-related protein (BRP) misc polyphenol oxidase (PPO) misc purification misc melon misc structural characterization misc Chemistry
topic_unstemmed	misc QD1-999 misc browning-related protein (BRP) misc polyphenol oxidase (PPO) misc purification misc melon misc structural characterization misc Chemistry
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title	Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino)
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title_full	Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino)
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title_sort	catalytic and structural characterization of a browning-related protein in oriental sweet melon (cucumis melo var. makuwa makino)
callnumber	QD1-999
title_auth	Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino)
abstract	Polyphenol oxidase (PPO) in plants plays an important role in browning reactions and may affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitation and column chromatography. The BRP possessed a high degree of identity with several chitinase proteins, particularly defense-related proteins, by MS identification. Pyrogallol was determined as the most appropriate substrate for BRP (Km = 0.04278 M). BRP exhibited extreme resistance under alkaline and high temperature conditions when pyrogallol was used as substrate. Polyacrylamide gel electrophoresis (PAGE) analysis indicated that BRP was a homo-dimer of two subunits and had a molecular weight of 37 kDa. Structural analysis indicated that the α-helix was the dominant conformation of BRP. The active site of the protein might be buried deeply in the protein, and BRP might be monodispersed in an aqueous system.
abstractGer	Polyphenol oxidase (PPO) in plants plays an important role in browning reactions and may affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitation and column chromatography. The BRP possessed a high degree of identity with several chitinase proteins, particularly defense-related proteins, by MS identification. Pyrogallol was determined as the most appropriate substrate for BRP (Km = 0.04278 M). BRP exhibited extreme resistance under alkaline and high temperature conditions when pyrogallol was used as substrate. Polyacrylamide gel electrophoresis (PAGE) analysis indicated that BRP was a homo-dimer of two subunits and had a molecular weight of 37 kDa. Structural analysis indicated that the α-helix was the dominant conformation of BRP. The active site of the protein might be buried deeply in the protein, and BRP might be monodispersed in an aqueous system.
abstract_unstemmed	Polyphenol oxidase (PPO) in plants plays an important role in browning reactions and may affect the quality of sweet melon products. In this study, a browning-related protein (BRP) with PPO activity was partially purified from oriental sweet melon (Cucumis melo var. makuwa Makino) by salt precipitation and column chromatography. The BRP possessed a high degree of identity with several chitinase proteins, particularly defense-related proteins, by MS identification. Pyrogallol was determined as the most appropriate substrate for BRP (Km = 0.04278 M). BRP exhibited extreme resistance under alkaline and high temperature conditions when pyrogallol was used as substrate. Polyacrylamide gel electrophoresis (PAGE) analysis indicated that BRP was a homo-dimer of two subunits and had a molecular weight of 37 kDa. Structural analysis indicated that the α-helix was the dominant conformation of BRP. The active site of the protein might be buried deeply in the protein, and BRP might be monodispersed in an aqueous system.
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title_short	Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino)
url	https://doi.org/10.3389/fchem.2018.00354 https://doaj.org/article/b94ad81dea274e1dbad61e786a16f9f8 https://www.frontiersin.org/article/10.3389/fchem.2018.00354/full https://doaj.org/toc/2296-2646
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Catalytic and Structural Characterization of a Browning-Related Protein in Oriental Sweet Melon (Cucumis Melo var. Makuwa Makino)

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