Immobilised Enzymes for Sesquiterpene Synthesis in Batch and Flow Systems

Donya Valikhani; Prabhakar Srivastava; Rudolf K Allemann; Thomas Wirth

doi:10.1002/cctc.201902135

Immobilised Enzymes for Sesquiterpene Synthesis in Batch and Flow Systems

Donya Valikhani
, Prabhakar Srivastava
, Rudolf K Allemann
, Thomas Wirth

School of Healthcare Sciences, Cardiff University

Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid

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Sesquiterpene synthases catalyse the bioconversion of farnesyl diphosphate into sesquiterpenes. The immobilisation of sesquiterpene synthases on controlled porosity glass through metal-ion affinity binding is reported. The immobilised sesquiterpene synthases were able to maintain 50 % catalytic activity for at least 50 cycles under continuous flow conditions.

Iaith wreiddiol	Saesneg
Cyfnodolyn	ChemCatChem
Cyfrol	12
Rhif cyhoeddi	8
Dyddiad ar-lein cynnar	21 Ion 2020
Dynodwyr Gwrthrych Digidol (DOIs)	https://doi.org/10.1002/cctc.201902135
Statws	Cyhoeddwyd - 20 Ebr 2020
Cyhoeddwyd yn allanol	Ie

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10.1002/cctc.201902135

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@article{e2b65b3925bb43d8b232b957c972af7d,

title = "Immobilised Enzymes for Sesquiterpene Synthesis in Batch and Flow Systems",

abstract = "Sesquiterpene synthases catalyse the bioconversion of farnesyl diphosphate into sesquiterpenes. The immobilisation of sesquiterpene synthases on controlled porosity glass through metal-ion affinity binding is reported. The immobilised sesquiterpene synthases were able to maintain 50 \% catalytic activity for at least 50 cycles under continuous flow conditions.",

author = "Donya Valikhani and Prabhakar Srivastava and Allemann, \{Rudolf K\} and Thomas Wirth",

year = "2020",

month = apr,

day = "20",

doi = "10.1002/cctc.201902135",

language = "English",

volume = "12",

journal = "ChemCatChem",

publisher = "Wiley",

number = "8",

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TY - JOUR

T1 - Immobilised Enzymes for Sesquiterpene Synthesis in Batch and Flow Systems

AU - Valikhani, Donya

AU - Srivastava, Prabhakar

AU - Allemann, Rudolf K

AU - Wirth, Thomas

PY - 2020/4/20

Y1 - 2020/4/20

N2 - Sesquiterpene synthases catalyse the bioconversion of farnesyl diphosphate into sesquiterpenes. The immobilisation of sesquiterpene synthases on controlled porosity glass through metal-ion affinity binding is reported. The immobilised sesquiterpene synthases were able to maintain 50 % catalytic activity for at least 50 cycles under continuous flow conditions.

AB - Sesquiterpene synthases catalyse the bioconversion of farnesyl diphosphate into sesquiterpenes. The immobilisation of sesquiterpene synthases on controlled porosity glass through metal-ion affinity binding is reported. The immobilised sesquiterpene synthases were able to maintain 50 % catalytic activity for at least 50 cycles under continuous flow conditions.

U2 - 10.1002/cctc.201902135

DO - 10.1002/cctc.201902135

M3 - Article

VL - 12

JO - ChemCatChem

JF - ChemCatChem

IS - 8

ER -

Immobilised Enzymes for Sesquiterpene Synthesis in Batch and Flow Systems

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