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Cloning and expression of a novel gene encoded thermostable archaeal aldolase class II from natural Sample
Suhartia,b, Meray N.W.a,c, Nurbaiti S.a, Akhmalokaa
a Biochemistry Research Group, Faculty of Mathematics and Natural Sciences, Institute Teknologi Bandung, Bandung, 40132, Indonesia
b Faculty of Pharmacy, Universitas 17 Agustus 1945 (UTA’45) Jakarta, Jl. Sunter Permai Raya, Sunter Agung Podomoro, Jakarta, Indonesia
c Department of Oil and Gas Processing Technology, Sekolah Tinggi Teknologi Minyakdan Gas, Balikpapan, Kalimantan Timur, Indonesia
[vc_row][vc_column][vc_row_inner][vc_column_inner][vc_separator css=”.vc_custom_1624529070653{padding-top: 30px !important;padding-bottom: 30px !important;}”][/vc_column_inner][/vc_row_inner][vc_row_inner layout=”boxed”][vc_column_inner width=”3/4″ css=”.vc_custom_1624695412187{border-right-width: 1px !important;border-right-color: #dddddd !important;border-right-style: solid !important;border-radius: 1px !important;}”][vc_empty_space][megatron_heading title=”Abstract” size=”size-sm” text_align=”text-left”][vc_column_text]A novel class II Aldolase was isolated through metagenomic approach from Domas Crater, West Java, Indonesia. Sequence analysis of the enzyme was highly homolog to archaeal ribulose-5-phosphate 4-epimerase from uncultured Acidilobussp. with percent identityof 63%. Homological analysis of the protein shows that the protein sequence contains all conserved motifs of aldolase class II. The enzyme shows Zn2+ binding, polypeptide binding, and active sites as other aldolase’s. Phylogenetic analysis of the enzyme showed that the enzyme makes a different branch closed to ribulose-5-phosphate 4-epimerase of unculcured Acidilobus sp. The gene was expressed in E coli as a host, and produced 26kDa of protein. Further analysis of the enzyme showed that the enzyme is thermostable. In addition, the enzymewas purified through Ion Metal Affinity Chromatography and it showed as single band with the homogeneity at around 96%.[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Author keywords” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Indexed keywords” size=”size-sm” text_align=”text-left”][vc_column_text]Aldolase,Cloning,Metagenomic approach,Thermostable[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Funding details” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”DOI” size=”size-sm” text_align=”text-left”][vc_column_text]https://doi.org/10.13005/bbra/1754[/vc_column_text][/vc_column_inner][vc_column_inner width=”1/4″][vc_column_text]Widget Plumx[/vc_column_text][/vc_column_inner][/vc_row_inner][/vc_column][/vc_row][vc_row][vc_column][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][/vc_column][/vc_row]