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ImmobilizedGlutamateDecarboxylasePreparationandOptimumConditionsofEnrichγ-AminobutyricAcid(PDF)

《南京师大学报(自然科学版)》[ISSN:1001-4616/CN:32-1239/N]

Issue:
2020年01期
Page:
107-114
Research Field:
·生物学·
Publishing date:

Info

Title:
ImmobilizedGlutamateDecarboxylasePreparationandOptimumConditionsofEnrichγ-AminobutyricAcid
Author(s):
LiuPingLiuPengliHuangChenYinZhimin
SchoolofLifeSciences,NanjingNormalUniversity,InstituteofBiochemistryandBiologicalProducts,JiangsuProvinceKeyLaboratoryforMolecularandMedicalBiotechnology,Nanjing210023,China
Keywords:
Carrageenanglutamatedecarboxylaseγ-aminobutyricacidimmobilizedenzyme
PACS:
TS201.3
DOI:
10.3969/j.issn.1001-4616.2020.01.016
Abstract:
Researchontheoptimumconditionsofimmobilizedglutamatedecarboxylasebycarrageenanandenrichγ-aminobutyricacid(GABA).Thegeneticallyengineeredbacteriaexpressingglutamatedecarboxylase(GAD)wereinducedbytheinducingagentwhichdevelopedbyourlaboratory,andthecrudeenzymesolutionobtainedbythestrainwasembedded-immobilizedwithCarrageenan.FactorswhichaffectedtheimmobilizationeffectofGADandtheyieldofGABAwereinvestigated.TheoptimumconcentrationofcarrageenanandKClwere1.5%and3%,solidifyingfor2h.TheoptimumpHwas3.8-4.3andthetemperaturewas37℃-43℃.Theimmobilizedglutamatedecarboxylase(IGAD)wasrepeatedlyusedafter7times,theactivitywaskeptashighas75%oftheinitial.ContinuousconversionofIGADtoprepareGABA,thereactionwascarriedoutattheoptimumsubstrateconcentrationof60mmol/L,thefinalmolarconversionofGABAwas70.98%,thecrystalyieldwas91.90%andthecrystalpuritywas94.73%.ThemethodhasgoodstabilityandhighsubstrateconversionratewhichmayprovideareferenceforcontinuouspreparationofGABA.

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Last Update: 2020-03-15