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Molecular Cloning and Expression of Candida antarctica lipase B in Corynebacterium genus
Tamara González,Hasna Nait M'Barek,Ahmed E. Gomaa,Hassan Hajjaj,Chen Zhen,Liu Dehua 한국미생물·생명공학회 2019 한국미생물·생명공학회지 Vol.47 No.4
This study, for the first time, reports the functional expression of lipase B derived from the yeast Candida antarctica (CALB) in Corynebacterium strain using the Escherichia coli plasmid PK18. The CALB gene fragment encoding a 317-amino-acid protein was successfully obtained from the total RNA of C. antarctica. CALB was readily produced in the Corynebacterium strain without the use of induction methods described in previous studies. This demonstrated the extracellular production of CALB in the Corynebacterium strain. CALB produced in the Corynebacterium MB001 strain transformed with pEC-CALB recombinant plasmid exhibited maximum extracellular enzymatic activity and high substrate affinity. The optimal pH and temperature for the hydrolysis of 4-nitrophenyl laurate by CALB were 9.0 and 40℃, respectively. The enzyme was stable at pH 10.7 in the glycine-KOH buffer and functioned as an alkaline lipase. The CALB activity was inhibited in the presence of high concentration of Mg2+, which indicated that CALB is not a metalloenzyme. These properties are key for the industrial application of the enzyme.
Molecular Cloning and Expression of Candida antarctica lipase B in Corynebacterium genus
Gonzalez, Tamara,M'Barek, Hasna Nait,Gomaa, Ahmed E.,Hajjaj, Hassan,Zhen, Chen,Dehua, Liu The Korean Society for Microbiology and Biotechnol 2019 한국미생물·생명공학회지 Vol.47 No.4
This study, for the first time, reports the functional expression of lipase B derived from the yeast Candida antarctica (CALB) in Corynebacterium strain using the Escherichia coli plasmid PK18. The CALB gene fragment encoding a 317-amino-acid protein was successfully obtained from the total RNA of C. antarctica. CALB was readily produced in the Corynebacterium strain without the use of induction methods described in previous studies. This demonstrated the extracellular production of CALB in the Corynebacterium strain. CALB produced in the Corynebacterium MB001 strain transformed with pEC-CALB recombinant plasmid exhibited maximum extracellular enzymatic activity and high substrate affinity. The optimal pH and temperature for the hydrolysis of 4-nitrophenyl laurate by CALB were 9.0 and 40℃, respectively. The enzyme was stable at pH 10.7 in the glycine-KOH buffer and functioned as an alkaline lipase. The CALB activity was inhibited in the presence of high concentration of Mg<sup>2+</sup>, which indicated that CALB is not a metalloenzyme. These properties are key for the industrial application of the enzyme.
Abdel-Alim Abdel-Alim Mohamed,EI-Shorbagi Abdel-Nasser Ahmed,Abdel-Moty Samia Galal,Abdel-Allah Hajjaj Hassan Mohamed The Pharmaceutical Society of Korea 2005 Archives of Pharmacal Research Vol.28 No.6
This work includes the synthesis of 15 final compounds (6a-h and 7b-h) as prod rugs of 5-ASA in the form of the acid itself, esters and amides linked by an amide linkage through a spacer to the endocyclic ring N of nicotinamide. Also, 15 new intermediate compounds were prepared. The target compounds (6b, 6f, 7b, and 7e-h) revealed potent analgesic and anti-inflammatory activities in comparison to sulfasalazine and 5-ASA. In addition, ulcerogenicity, $LD_{50}$, in vivo and in vitro metabolism of compound 7f were determined.
Abdel-Alim Mohamed Abdel-Alim,Abdel-Nasser Ahmed El-Shorbagi,Samia Galal Abdel-Moty,Hajjaj Hassan Mohamed Abdel-Allah 대한약학회 2005 Archives of Pharmacal Research Vol.28 No.6
This work includes the synthesis of 15 final compounds (6a-h and 7b-h) as prodrugs of 5-ASA in the form of the acid itself, esters and amides linked by an amide linkage through a spacer to the endocyclic ring N of nicotinamide. Also, 15 new intermediate compounds were prepared. The target compounds (6b, 6f, 7b, and 7e-h) revealed potent analgesic and anti-inflammatory activities in comparison to sulfasalazine and 5-ASA. In addition, ulcerogenicity, LD50, in vivo and in vitro metabolism of compound 7f were determined.