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Babich O.O. , Kemerovo Institute of Food Science and Technology , bul`v. Stroitelei 47, Kemerovo, 650056 Russia , olich.43@mail.ru

Dyshlyuk L. , Kemerovo Institute of Food Science and Technology , bul`v. Stroitelei 47, Kemerovo, 650056 Russia

Milent`eva I.S. , Kemerovo Institute of Food Science and Technology , bul`v. Stroitelei 47, Kemerovo, 650056 Russia

Год 2013 Номер журнала 1 DOI 577.112.387.2
Аннотация The pal gene coding for L-phenylalanine ammonia-lyase of Rhodosporidium toruloides (GenBank entry no. X12702.1) with optimized sequence was cloned into an expressing vector pET28a. Three parameters of expression (inductor type, duration, and temperature of induction) were optimized, which resulted in a strain producing recombinant L-phenylalanine ammonia-lyase with the maximal productivity, that is, 35 В± 1% to total cell protein, upon utilization of 0.2% lactose (according to Studier) induction during 18 h at 37В°C. The recombinant L-phenylalanine ammonia-lyase was found to be insoluble by 99%. Solubility of the protein did not improve upon utilization of 1 mM IPTG as an inductor instead of 0.2% lactose, or upon bacterium cultivation at various temperatures, that is 25В°C and 37В°C.
Ключевые слова L-phenylalanine ammonia-lyase, cloning, expression, recombinant protein, induction, L-phenylalanine, phenylketonuria
Информация о статье Дата поступления 30 ноября -0001 года
Дата принятия в печать 30 ноября -0001 года
Дата онлайн-размещения 30 ноября -0001 года
Выходные данные статьи Babich O.O. EXPRESSION OF RECOMBINANT L-PHENYLALANINE AMMONIA-LYASE IN ESCHERICHIA COLI / Babich O.O., Dyshlyuk L., Milent`eva I.S. // Food and Raw Materials. - 2013. - №1. - С. 48-53
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