The Screening of Alcohol Dehydrogenase (ADH) Mutant of Rhizopus oryzae / 微生物学通报
Microbiology
; (12)1992.
Article
em Zh
| WPRIM
| ID: wpr-685311
Biblioteca responsável:
WPRO
ABSTRACT
During L-lactic acid fermentation with Rhizopus oryzae,there existed a branch pathway by which pyruvate was transformed to eth- anol catalyzed by pyruvate decarboxylase(PDC)and alcohol dehydrogenase(ADH),thus decreasing the flux of pyruvate to lactic acid.In this study,the spores of Rhizopus oryzae AS3.3462 mutagenized with nitrosoguanidine(NTG),the appropriate dosage was 0.15 mg/mL and the lethal rate was 70%~80%.Two mutants,named mut-1 and mut-2,with decreased ADH activity were screened out by yeast peptone dextrose(YPD)agar medium containing allyl alcohol.These two mutants had decreased ADH activities of 41.63% and 50.29% compared with the parent strain.The fermentation behavior after 72h showed that the yields of ethanol produced by mut-1 and mut-2 were 4.87g/L and 6.56g/L respectively,while the wild type strain was 28.9g/L,and the lactate concentrations of mut-1 and mut-2 also increased from 40.31g/L to 54.45g/L and 44.07 g/L,respectively.It is also found that mut-1 and mut-2 had a high reducing sugar consumption rate and biomass accumulation than its present strain
Texto completo:
1
Base de dados:
WPRIM
Tipo de estudo:
Diagnostic_studies
/
Screening_studies
Idioma:
Zh
Revista:
Microbiology
Ano de publicação:
1992
Tipo de documento:
Article