Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials

Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the...
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Autor*in:	Almulaiky, Yaaser Q. [verfasserIn] Almaghrabi, Omar

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	Polyphenol oxidase Purification Immobilization Nanocomposite materials

Anmerkung:	© The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022

Übergeordnetes Werk:	Enthalten in: Catalysis letters - Dordrecht [u.a.] : Springer Science + Business Media B.V, 1988, 152(2022), 10 vom: 07. Jan., Seite 3089-3099
Übergeordnetes Werk:	volume:152 ; year:2022 ; number:10 ; day:07 ; month:01 ; pages:3089-3099

Links:	Volltext

DOI / URN:	10.1007/s10562-022-03916-5

Katalog-ID:	SPR048258040

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245	1	0	\|a Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials
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520			\|a Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract
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allfields	10.1007/s10562-022-03916-5 doi (DE-627)SPR048258040 (SPR)s10562-022-03916-5-e DE-627 ger DE-627 rakwb eng Almulaiky, Yaaser Q. verfasserin aut Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022 Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract Polyphenol oxidase (dpeaa)DE-He213 Purification (dpeaa)DE-He213 Immobilization (dpeaa)DE-He213 Nanocomposite materials (dpeaa)DE-He213 Almaghrabi, Omar aut Enthalten in Catalysis letters Dordrecht [u.a.] : Springer Science + Business Media B.V, 1988 152(2022), 10 vom: 07. Jan., Seite 3089-3099 (DE-627)306717638 (DE-600)1501518-X 1572-879X nnns volume:152 year:2022 number:10 day:07 month:01 pages:3089-3099 https://dx.doi.org/10.1007/s10562-022-03916-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 152 2022 10 07 01 3089-3099
spelling	10.1007/s10562-022-03916-5 doi (DE-627)SPR048258040 (SPR)s10562-022-03916-5-e DE-627 ger DE-627 rakwb eng Almulaiky, Yaaser Q. verfasserin aut Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022 Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract Polyphenol oxidase (dpeaa)DE-He213 Purification (dpeaa)DE-He213 Immobilization (dpeaa)DE-He213 Nanocomposite materials (dpeaa)DE-He213 Almaghrabi, Omar aut Enthalten in Catalysis letters Dordrecht [u.a.] : Springer Science + Business Media B.V, 1988 152(2022), 10 vom: 07. Jan., Seite 3089-3099 (DE-627)306717638 (DE-600)1501518-X 1572-879X nnns volume:152 year:2022 number:10 day:07 month:01 pages:3089-3099 https://dx.doi.org/10.1007/s10562-022-03916-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 152 2022 10 07 01 3089-3099
allfields_unstemmed	10.1007/s10562-022-03916-5 doi (DE-627)SPR048258040 (SPR)s10562-022-03916-5-e DE-627 ger DE-627 rakwb eng Almulaiky, Yaaser Q. verfasserin aut Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022 Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract Polyphenol oxidase (dpeaa)DE-He213 Purification (dpeaa)DE-He213 Immobilization (dpeaa)DE-He213 Nanocomposite materials (dpeaa)DE-He213 Almaghrabi, Omar aut Enthalten in Catalysis letters Dordrecht [u.a.] : Springer Science + Business Media B.V, 1988 152(2022), 10 vom: 07. Jan., Seite 3089-3099 (DE-627)306717638 (DE-600)1501518-X 1572-879X nnns volume:152 year:2022 number:10 day:07 month:01 pages:3089-3099 https://dx.doi.org/10.1007/s10562-022-03916-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 152 2022 10 07 01 3089-3099
allfieldsGer	10.1007/s10562-022-03916-5 doi (DE-627)SPR048258040 (SPR)s10562-022-03916-5-e DE-627 ger DE-627 rakwb eng Almulaiky, Yaaser Q. verfasserin aut Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022 Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract Polyphenol oxidase (dpeaa)DE-He213 Purification (dpeaa)DE-He213 Immobilization (dpeaa)DE-He213 Nanocomposite materials (dpeaa)DE-He213 Almaghrabi, Omar aut Enthalten in Catalysis letters Dordrecht [u.a.] : Springer Science + Business Media B.V, 1988 152(2022), 10 vom: 07. Jan., Seite 3089-3099 (DE-627)306717638 (DE-600)1501518-X 1572-879X nnns volume:152 year:2022 number:10 day:07 month:01 pages:3089-3099 https://dx.doi.org/10.1007/s10562-022-03916-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 152 2022 10 07 01 3089-3099
allfieldsSound	10.1007/s10562-022-03916-5 doi (DE-627)SPR048258040 (SPR)s10562-022-03916-5-e DE-627 ger DE-627 rakwb eng Almulaiky, Yaaser Q. verfasserin aut Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022 Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract Polyphenol oxidase (dpeaa)DE-He213 Purification (dpeaa)DE-He213 Immobilization (dpeaa)DE-He213 Nanocomposite materials (dpeaa)DE-He213 Almaghrabi, Omar aut Enthalten in Catalysis letters Dordrecht [u.a.] : Springer Science + Business Media B.V, 1988 152(2022), 10 vom: 07. Jan., Seite 3089-3099 (DE-627)306717638 (DE-600)1501518-X 1572-879X nnns volume:152 year:2022 number:10 day:07 month:01 pages:3089-3099 https://dx.doi.org/10.1007/s10562-022-03916-5 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 152 2022 10 07 01 3089-3099
language	English
source	Enthalten in Catalysis letters 152(2022), 10 vom: 07. Jan., Seite 3089-3099 volume:152 year:2022 number:10 day:07 month:01 pages:3089-3099
sourceStr	Enthalten in Catalysis letters 152(2022), 10 vom: 07. Jan., Seite 3089-3099 volume:152 year:2022 number:10 day:07 month:01 pages:3089-3099
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Polyphenol oxidase Purification Immobilization Nanocomposite materials
isfreeaccess_bool	false
container_title	Catalysis letters
authorswithroles_txt_mv	Almulaiky, Yaaser Q. @@aut@@ Almaghrabi, Omar @@aut@@
publishDateDaySort_date	2022-01-07T00:00:00Z
hierarchy_top_id	306717638
id	SPR048258040
language_de	englisch
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PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. 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author	Almulaiky, Yaaser Q.
spellingShingle	Almulaiky, Yaaser Q. misc Polyphenol oxidase misc Purification misc Immobilization misc Nanocomposite materials Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials
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topic_title	Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials Polyphenol oxidase (dpeaa)DE-He213 Purification (dpeaa)DE-He213 Immobilization (dpeaa)DE-He213 Nanocomposite materials (dpeaa)DE-He213
topic	misc Polyphenol oxidase misc Purification misc Immobilization misc Nanocomposite materials
topic_unstemmed	misc Polyphenol oxidase misc Purification misc Immobilization misc Nanocomposite materials
topic_browse	misc Polyphenol oxidase misc Purification misc Immobilization misc Nanocomposite materials
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title	Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials
ctrlnum	(DE-627)SPR048258040 (SPR)s10562-022-03916-5-e
title_full	Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials
author_sort	Almulaiky, Yaaser Q.
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author_browse	Almulaiky, Yaaser Q. Almaghrabi, Omar
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doi_str_mv	10.1007/s10562-022-03916-5
title_sort	polyphenol oxidase from coleus forskohlii: purification, characterization, and immobilization onto alginate/zno nanocomposite materials
title_auth	Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials
abstract	Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022
abstractGer	Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022
abstract_unstemmed	Abstract Herein, polyphenol oxidase (PPO) was purified from Coleus forskohlii via a three-step process involving precipitation by ($ NH_{4} $)2$ SO_{4} $, ion exchange chromatography and gel filtration. PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. Graphical Abstract © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2022
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title_short	Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials
url	https://dx.doi.org/10.1007/s10562-022-03916-5
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up_date	2024-07-03T18:03:14.796Z
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PPO was purified 15-fold with a total yield of 31% and a specific activity of 3168 U/mg, and the observed molecular weight was 42 kDa. To improve the reusability and stability of the purified enzyme, calcium alginate incorporated with zinc oxide nanoparticles (Ca-ALG-ZnO NPs) was successfully prepared and characterized through scanning electron microscopy and Fourier transform infrared spectroscopy and utilized as a support for PPO immobilization. The immobilization yield and enzyme activity reached 83% and 3950 U/g support, respectively. The results showed that immobilized PPO could be reused ten times while retaining 69% of its original activity. The purified and immobilized PPO exhibited an optimal pH of 7.0 and 7.5 and an optimal temperature of 40 °C and 50 °C, respectively. The purified and immobilized PPO showed Vmax values of 255.75 and 251.89 Units/ml, and Km values of 4.99 and 3.12 mM, respectively. As a result, this work provides an opportunity to understand and manage the influence of the coleus forskohlii PPO enzyme in key immobilization, industrial. Additionally, the results indicated that the Ca-ALG-ZnO NPs used as supports had a significant effect on the enzyme activity and stability of immobilized PPO. 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Polyphenol Oxidase from Coleus forskohlii: Purification, Characterization, and Immobilization Onto Alginate/ZnO Nanocomposite Materials

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