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      저자 : Hasna Nait M'Barek (검색결과 2 건)
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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.

      • SCOPUSKCI등재

        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.

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