An approach to recombinantly produce mature grape polyphenol oxidase

Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Li, Yu [verfasserIn] McLarin, Mark-Anthony [verfasserIn] Middleditch, Martin J. [verfasserIn] Morrow, Stuart J. [verfasserIn] Kilmartin, Paul A. [verfasserIn] Leung, Ivanhoe K.H. [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Schlagwörter:	Polyphenol oxidase Shine Muscat Grape Recombinant protein Protein expression and purification

Übergeordnetes Werk:	Enthalten in: Biochimie - Paris [u.a.] : Elsevier, 1971, 165, Seite 40-47
Übergeordnetes Werk:	volume:165 ; pages:40-47

DOI / URN:	10.1016/j.biochi.2019.07.002

Katalog-ID:	ELV002865130

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245	1	0	\|a An approach to recombinantly produce mature grape polyphenol oxidase
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520			\|a Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme.
650		4	\|a Polyphenol oxidase
650		4	\|a Shine Muscat
650		4	\|a Grape
650		4	\|a Recombinant protein
650		4	\|a Protein expression and purification
700	1		\|a McLarin, Mark-Anthony \|e verfasserin \|4 aut
700	1		\|a Middleditch, Martin J. \|e verfasserin \|4 aut
700	1		\|a Morrow, Stuart J. \|e verfasserin \|4 aut
700	1		\|a Kilmartin, Paul A. \|e verfasserin \|4 aut
700	1		\|a Leung, Ivanhoe K.H. \|e verfasserin \|0 (orcid)0000-0003-0633-6771 \|4 aut
773	0	8	\|i Enthalten in \|t Biochimie \|d Paris [u.a.] : Elsevier, 1971 \|g 165, Seite 40-47 \|h Online-Ressource \|w (DE-627)320496945 \|w (DE-600)2011725-5 \|w (DE-576)094142157 \|7 nnns
773	1	8	\|g volume:165 \|g pages:40-47
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936	b	k	\|a 35.70 \|j Biochemie: Allgemeines
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author_variant	y l yl m a m mam m j m mj mjm s j m sj sjm p a k pa pak i k l ik ikl
matchkey_str	liyumclarinmarkanthonymiddleditchmartinj:2019----:nprahoeobnnlpoueauerpp
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allfields	10.1016/j.biochi.2019.07.002 doi (DE-627)ELV002865130 (ELSEVIER)S0300-9084(19)30193-2 DE-627 ger DE-627 rda eng 540 DE-600 35.70 bkl Li, Yu verfasserin aut An approach to recombinantly produce mature grape polyphenol oxidase 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme. Polyphenol oxidase Shine Muscat Grape Recombinant protein Protein expression and purification McLarin, Mark-Anthony verfasserin aut Middleditch, Martin J. verfasserin aut Morrow, Stuart J. verfasserin aut Kilmartin, Paul A. verfasserin aut Leung, Ivanhoe K.H. verfasserin (orcid)0000-0003-0633-6771 aut Enthalten in Biochimie Paris [u.a.] : Elsevier, 1971 165, Seite 40-47 Online-Ressource (DE-627)320496945 (DE-600)2011725-5 (DE-576)094142157 nnns volume:165 pages:40-47 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines AR 165 40-47
spelling	10.1016/j.biochi.2019.07.002 doi (DE-627)ELV002865130 (ELSEVIER)S0300-9084(19)30193-2 DE-627 ger DE-627 rda eng 540 DE-600 35.70 bkl Li, Yu verfasserin aut An approach to recombinantly produce mature grape polyphenol oxidase 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme. Polyphenol oxidase Shine Muscat Grape Recombinant protein Protein expression and purification McLarin, Mark-Anthony verfasserin aut Middleditch, Martin J. verfasserin aut Morrow, Stuart J. verfasserin aut Kilmartin, Paul A. verfasserin aut Leung, Ivanhoe K.H. verfasserin (orcid)0000-0003-0633-6771 aut Enthalten in Biochimie Paris [u.a.] : Elsevier, 1971 165, Seite 40-47 Online-Ressource (DE-627)320496945 (DE-600)2011725-5 (DE-576)094142157 nnns volume:165 pages:40-47 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines AR 165 40-47
allfields_unstemmed	10.1016/j.biochi.2019.07.002 doi (DE-627)ELV002865130 (ELSEVIER)S0300-9084(19)30193-2 DE-627 ger DE-627 rda eng 540 DE-600 35.70 bkl Li, Yu verfasserin aut An approach to recombinantly produce mature grape polyphenol oxidase 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme. Polyphenol oxidase Shine Muscat Grape Recombinant protein Protein expression and purification McLarin, Mark-Anthony verfasserin aut Middleditch, Martin J. verfasserin aut Morrow, Stuart J. verfasserin aut Kilmartin, Paul A. verfasserin aut Leung, Ivanhoe K.H. verfasserin (orcid)0000-0003-0633-6771 aut Enthalten in Biochimie Paris [u.a.] : Elsevier, 1971 165, Seite 40-47 Online-Ressource (DE-627)320496945 (DE-600)2011725-5 (DE-576)094142157 nnns volume:165 pages:40-47 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines AR 165 40-47
allfieldsGer	10.1016/j.biochi.2019.07.002 doi (DE-627)ELV002865130 (ELSEVIER)S0300-9084(19)30193-2 DE-627 ger DE-627 rda eng 540 DE-600 35.70 bkl Li, Yu verfasserin aut An approach to recombinantly produce mature grape polyphenol oxidase 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme. Polyphenol oxidase Shine Muscat Grape Recombinant protein Protein expression and purification McLarin, Mark-Anthony verfasserin aut Middleditch, Martin J. verfasserin aut Morrow, Stuart J. verfasserin aut Kilmartin, Paul A. verfasserin aut Leung, Ivanhoe K.H. verfasserin (orcid)0000-0003-0633-6771 aut Enthalten in Biochimie Paris [u.a.] : Elsevier, 1971 165, Seite 40-47 Online-Ressource (DE-627)320496945 (DE-600)2011725-5 (DE-576)094142157 nnns volume:165 pages:40-47 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines AR 165 40-47
allfieldsSound	10.1016/j.biochi.2019.07.002 doi (DE-627)ELV002865130 (ELSEVIER)S0300-9084(19)30193-2 DE-627 ger DE-627 rda eng 540 DE-600 35.70 bkl Li, Yu verfasserin aut An approach to recombinantly produce mature grape polyphenol oxidase 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme. Polyphenol oxidase Shine Muscat Grape Recombinant protein Protein expression and purification McLarin, Mark-Anthony verfasserin aut Middleditch, Martin J. verfasserin aut Morrow, Stuart J. verfasserin aut Kilmartin, Paul A. verfasserin aut Leung, Ivanhoe K.H. verfasserin (orcid)0000-0003-0633-6771 aut Enthalten in Biochimie Paris [u.a.] : Elsevier, 1971 165, Seite 40-47 Online-Ressource (DE-627)320496945 (DE-600)2011725-5 (DE-576)094142157 nnns volume:165 pages:40-47 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.70 Biochemie: Allgemeines AR 165 40-47
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topic_facet	Polyphenol oxidase Shine Muscat Grape Recombinant protein Protein expression and purification
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authorswithroles_txt_mv	Li, Yu @@aut@@ McLarin, Mark-Anthony @@aut@@ Middleditch, Martin J. @@aut@@ Morrow, Stuart J. @@aut@@ Kilmartin, Paul A. @@aut@@ Leung, Ivanhoe K.H. @@aut@@
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author	Li, Yu
spellingShingle	Li, Yu ddc 540 bkl 35.70 misc Polyphenol oxidase misc Shine Muscat misc Grape misc Recombinant protein misc Protein expression and purification An approach to recombinantly produce mature grape polyphenol oxidase
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topic_title	540 DE-600 35.70 bkl An approach to recombinantly produce mature grape polyphenol oxidase Polyphenol oxidase Shine Muscat Grape Recombinant protein Protein expression and purification
topic	ddc 540 bkl 35.70 misc Polyphenol oxidase misc Shine Muscat misc Grape misc Recombinant protein misc Protein expression and purification
topic_unstemmed	ddc 540 bkl 35.70 misc Polyphenol oxidase misc Shine Muscat misc Grape misc Recombinant protein misc Protein expression and purification
topic_browse	ddc 540 bkl 35.70 misc Polyphenol oxidase misc Shine Muscat misc Grape misc Recombinant protein misc Protein expression and purification
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title	An approach to recombinantly produce mature grape polyphenol oxidase
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title_full	An approach to recombinantly produce mature grape polyphenol oxidase
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author_browse	Li, Yu McLarin, Mark-Anthony Middleditch, Martin J. Morrow, Stuart J. Kilmartin, Paul A. Leung, Ivanhoe K.H.
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title_sort	an approach to recombinantly produce mature grape polyphenol oxidase
title_auth	An approach to recombinantly produce mature grape polyphenol oxidase
abstract	Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme.
abstractGer	Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme.
abstract_unstemmed	Polyphenol oxidases (PPOs) are important enzymes that are widely found in both prokaryotes and eukaryotes including grapes. Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. Our work provides a simple protocol of obtaining pure and active recombinant grape PPO that will enable further studies about the catalytic mechanism and inhibition of this enzyme.
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title_short	An approach to recombinantly produce mature grape polyphenol oxidase
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author2	McLarin, Mark-Anthony Middleditch, Martin J. Morrow, Stuart J. Kilmartin, Paul A. Leung, Ivanhoe K.H.
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doi_str	10.1016/j.biochi.2019.07.002
up_date	2024-07-06T17:42:54.375Z
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Studies of grape PPO to date have mostly relied on enzymes extracted and purified from plants. In this work, we describe the production of the mature form of Shine Muscat grape PPO by using an Escherichia coli expression system. We have optimised the purification procedure to obtain pure and active recombinant enzymes and characterised the catalytic efficiency of the recombinant grape PPO by using ultraviolet/visible (UV/Vis) spectrophotometry. 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An approach to recombinantly produce mature grape polyphenol oxidase

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