Tyrosinase-containing chitosan gels: A combined catalyst and sorbent for selective phenol removal

Sun, Wei‐Qiang; Payne, Gregory F.

doi:10.1002/(sici)1097-0290(19960705)51:1<79::aid-bit9>3.0.co;2-y

Cited by 60 publications

(41 citation statements)

References 17 publications

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“…Tel: +81-47-474-2571; Fax: +81-47-474-2579; E-mail: k5yamada@cit.nihon-u.ac.jp remove tyrosinase-generated quinone derivatives has been reported by some researchers. 11,27,28) Their results indicate that the combination of tyrosinase and cationic polymer coagulants is an effective procedure in removing carcinogenic phenol compounds from aqueous solutions. But, one of the major problems in this procedure is that there is an optimum concentration range of the coagulant for maximum flocculation.…”

mentioning

confidence: 99%

Removal ofp-Alkylphenols from Aqueous Solutions by Combined Use of Mushroom Tyrosinase and Chitosan Beads

Yamada

Inoue

Akiba

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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confidence: 99%

Removal ofp-Alkylphenols from Aqueous Solutions by Combined Use of Mushroom Tyrosinase and Chitosan Beads

Yamada

Inoue

Akiba

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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“…Tyrosinase activity was measured by modifying the method described by Sun [7], using 50 mM sodiumphosphate buffer (pH 7) as relative activity. The culture filtrate was centrifuged at 7200 rpm for 15 min and used as the enzyme sample.…”

Section: Enzyme Activity Assaymentioning

confidence: 99%

Stability of Tyrosinase Enzyme from Funalia Trogii

Majidi¹,

Aksöz²

2013

AJMR

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Tyrosinases are widely distributed in nature; These enzymes are known as type 3 copper proteins having a diamagnetic spin-coupled copper pair in the active centre. In this study, the objective was to produce stable tyrosinase enzyme efficiently and determine stability of enzyme from an alternative fungal soruce, Funalia trogii. Temperature and pH stabilities of the crude extract of enzyme were studied and it was concluded that crude extract of tyrosinase was stable at 73º C . pH stability of tyrosinase enzyme was among 3,5-7 ranges.

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“…It might be expected that an increase in the loading of immobilized tyrosinase would lead to an increase in phenol removal rate; however, the relationship between these two variables is not linear. Similar results were observed by Sun and Payne [10]. The authors argued that, when the tyrosinase to chitosan ratio was increased, the rate of o-quinone formation was enhanced with an increase in the localized o-quinone concentration.…”

Section: Immobilized Enzyme Loadingmentioning

confidence: 99%

“…Chitosan is a suitable material for sorption and enzyme immobilization, and has been used for the immobilization of such enzymes as acid phosphatase, b-glucosidase and tyrosinase [10][11][12]. It has also been used in a chitosan-coated polysulphone capillary membrane system for the bioremediation of phenolic effluents [13].…”

Section: Introductionmentioning

confidence: 99%

“…Chitosan as a support matrix is also robust enough to tolerate moderate hydrodynamic shear, which makes it a suitable matrix for use under fluidized reactor conditions. Several researchers [10,[14][15][16] have investigated the use of enzymes with lab-scale reactors. However, applications of this technology in a larger, three-phase fluidized bed reactor have not been conducted.…”

Section: Introductionmentioning

confidence: 99%

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Removal of aqueous phenol using immobilized enzymes in a bench scale and pilot scale three-phase fluidized bed reactor

Ensuncho

Alvarez-Cuenca

Legge

2005

Bioprocess Biosyst Eng

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The main objective of this work was to investigate the removal of aqueous phenol using immobilized enzymes in both bench scale and pilot scale three-phase fluidized bed reactors. The enzyme used in this application was a fungal tyrosinase [E.C. 1.14.18.1] immobilized in a system of chitosan and alginate. The immobilization matrix consisted of a chitosan matrix cross-linked with glutaraldehyde with an aliginate-filled pore space. This support matrix showed superior mechanical properties along with retaining the unique adsorptive characteristics of the chitosan. Adsorption of the o-quinone product by the chitosan reduced tyrosinase inactivation that is normally observed for this enzyme under these conditions. This approach allowed reuse of the enzyme in repeated batch applications. For the bench scale reactor (1.2-l capacity) more than 92% of the phenol could be removed from the feed water using an immobilized enzyme volume of 18.5% and a residence time of the liquid phase of 150 min. Removal rates decreased with subsequent batch runs. For the pilot scale fluidized bed (60 l), 60% phenol removal was observed with an immobilized enzyme volume of 5% and a residence time of the liquid phase of 7 h. Removal decreased to 45% with a repeat batch run with the same immobilized enzyme.

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Tyrosinase-containing chitosan gels: A combined catalyst and sorbent for selective phenol removal

Cited by 60 publications

References 17 publications

Removal ofp-Alkylphenols from Aqueous Solutions by Combined Use of Mushroom Tyrosinase and Chitosan Beads

Removal ofp-Alkylphenols from Aqueous Solutions by Combined Use of Mushroom Tyrosinase and Chitosan Beads

Stability of Tyrosinase Enzyme from <i>Funalia </i><i>T</i><i>rogii</i>

Removal of aqueous phenol using immobilized enzymes in a bench scale and pilot scale three-phase fluidized bed reactor

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