Purification and characterization of cell wall-bound peroxidase from vanilla bean

Márquez, Ofelia; Waliszewski, Krzysztof N.; Oliart-Ros, Rosa María; Pardío, Violeta T.

doi:10.1016/j.lwt.2007.08.017

Cited by 49 publications

(52 citation statements)

References 31 publications

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“…The peroxidases of pineapples were also found to be thermo-stable retaining residual activity higher than 60% after 30 minutes of treatment at 60 °C and becoming inactive only at 80 °C (BRITO et al, 2005). The peroxidases of vanilla were stable at temperatures below 30 °C (maintaining more than 60% of their activity) but became completely inactive at 70 °C at pH = 11.0 (MARQUEZ et al, 2008).…”

Section: Determination Of Peroxidase and Polyphenol-oxidase Activitiesmentioning

confidence: 99%

“…remained stable not appear to be exceptional since the peroxidase activity in two different pineapple varieties (BRITO et al, 2005) were higher than 90% in the pH range of 4.0 to 9.0 after incubation for 24 hours at 50 °C. The peroxidases of vanilla retained more than 60% of their activity when maintained at pH values between 5.0 and 12.0 (MARQUEZ et al, 2008).…”

Section: Determination Of Peroxidase and Polyphenol-oxidase Activitiesmentioning

confidence: 99%

“…were found to be stable in the pH range from 3.0 to 10.0, and the residual activity remained mostly above 60% (Figure 2). The high pH stability found does (MARQUEZ et al, 2008) and Copaifera langsdorffii leaves (MACIEL; GOUVÊA; PASTORE, 2006) demonstrate optimal levels of activity at pH 4.5, 3.8 and 5.5 respectively. However, the peroxidases of the kiwifruit demonstrate optimal activity values in the pH range between 6.0 and 8.5 (FANG et al, 2008).…”

Section: Determination Of Peroxidase and Polyphenol-oxidase Activitiesmentioning

confidence: 99%

“…The optimal temperature for the peroxidase activity in other plants is apparently extremely variable, with values of 50 °C being registered for two different varieties of pineapples (BRITO et al, 2005) but 16 °C for vanilla (MARQUEZ et al, 2008).…”

Section: Determination Of Peroxidase and Polyphenol-oxidase Activitiesmentioning

confidence: 99%

“…Peroxidases are known for their thermo stability, usually requiring rigorous thermal treatment to be inactivated. This type of treatment generally causes undesirable alterations in the products and should be limited to only the minimum necessary (SERRANO-MARTÍNEZ et al, 2008;MARQUEZ et al, 2008;SHALINI;SHIVHARE;BASU, 2008;WHITAKER, 1994). Polyphenol-oxidases are the main enzymes responsible for the enzymatic browning of plant tissues.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Partial characterization and inactivation of peroxidases and polyphenol-oxidases of umbu-cajá (Spondias spp.)

Silva¹,

Koblitz²

2010

Ciênc. Tecnol. Aliment.

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Section: Determination Of Peroxidase and Polyphenol-oxidase Activitiesmentioning

confidence: 99%

Section: Determination Of Peroxidase and Polyphenol-oxidase Activitiesmentioning

confidence: 99%

Section: Determination Of Peroxidase and Polyphenol-oxidase Activitiesmentioning

confidence: 99%

Section: Determination Of Peroxidase and Polyphenol-oxidase Activitiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Partial characterization and inactivation of peroxidases and polyphenol-oxidases of umbu-cajá (Spondias spp.)

Silva¹,

Koblitz²

2010

Ciênc. Tecnol. Aliment.

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A new xanthene‐based two‐photon fluorescent probe for the imaging of 1,4‐dithiothreitol (DTT) in living cells

et al. 2018

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1,4-Dithiothreitol (DTT) has wide applications in cell biology and biochemistry. Development of effective methods for monitoring DTT in biological systems is important for the safe handling and study of toxicity to humans. Herein, we describe a two-photon fluorescence probe (Rh-DTT) to detect DTT in living systems for the first time. Rh-DTT showed high selectivity and sensitivity to DTT. Rh-DTT can be successfully used for the two-photon imaging of DTT in living cells, and also can detect DTT in living tissues and mice.

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Use of partially purified peroxidase of agricultural by‐product rice bran in deoxynivalenol reduction

Gautério

Malta

Reginatto

et al. 2017

J of Chemical Tech & Biotech

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BACKGROUND Once peroxidase purification can improve substrate degradation capacity, peroxidase from rice bran was purified by expanded bed adsorption (EBA) coupled to diafiltration/ultrafiltration (DF/UF) and applied for deoxynivalenol (DON) reduction. RESULTS The DF/UF step was optimized according to membrane molecular weight cutoff (MWCO), DF cycles number, operation temperature and CaCl2 addition to the DF buffer. DON reduction tests were carried out with both clarified and purified peroxidase. The use of MWCO of 10 kDa, 10 °C, six DF cycles and adding 4 mmol L−1 CaCl2 to DF buffer promoted enzyme purification of 4.4‐fold and enzymatic recovery of 79.4%. The global purification process combining two techniques resulted in enzyme purification of 75.1‐fold with an enzymatic recovery of 22.8%. Peroxidase purified by EBA combined with DF/UF resulted in DON reduction of 81.7% in a model system. CONCLUSION Peroxidase purification was achieved by scale‐up integrated strategies. The use of purified peroxidase from agricultural by‐products could be a promising alternative for enzymatic DON levels reduction. © 2017 Society of Chemical Industry

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Purification and characterization of cell wall-bound peroxidase from vanilla bean

Cited by 49 publications

References 31 publications

Partial characterization and inactivation of peroxidases and polyphenol-oxidases of umbu-cajá (Spondias spp.)

Partial characterization and inactivation of peroxidases and polyphenol-oxidases of umbu-cajá (Spondias spp.)

A new xanthene‐based two‐photon fluorescent probe for the imaging of 1,4‐dithiothreitol (DTT) in living cells

Use of partially purified peroxidase of agricultural by‐product rice bran in deoxynivalenol reduction

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