{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Song W"],"funding":["Science and Technology Project Founded by Education Department of Jiangxi Province","National Natural Science Foundation of China"],"pagination":["84"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9925633"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(3)"],"pubmed_abstract":["In this paper, the cgt gene encoding cyclodextrin glycosyltransferase (CGTase) from <i>Bacillus stearothermophilus</i> was cloned into pWB980 plasmid for extracellular expression in <i>Bacillus subtilis</i> SCK6. Through adding a six-histidine affinity tag fused to the C-terminus, the recombinant CGTase could be purified by nickel ion affinity chromatography, and its molecular weight was approximately 76 kDa on SDS-PAGE. Then, the enzymatic properties were determined, and results were as follows: the optimum temperature and pH were identified as 40 ℃ and pH 5.0, respectively. CGTase had good tolerance to metal ions of Mn<sup>2+</sup>, Ca<sup>2+</sup>, and Mg<sup>2+</sup>. The enzyme activity was activated by Na<sup>+</sup>, Al<sup>3+</sup>, Fe<sup>3+</sup>, and Ni<sup>+</sup>, and it was r"],"journal":["3 Biotech"],"pubmed_title":["Heterologous expression of cyclodextrin glycosyltransferase from <i>Bacillus stearothermophilus</i> in <i>Bacillus subtilis</i> and its application in glycosyl rutin production."],"pmcid":["PMC9925633"],"funding_grant_id":["GJJ202305","31600639"],"pubmed_authors":["Li X","Zheng J","Zhang Y","Zhang M","Song W"],"additional_accession":[]},"is_claimable":false,"name":"Heterologous expression of cyclodextrin glycosyltransferase from <i>Bacillus stearothermophilus</i> in <i>Bacillus subtilis</i> and its application in glycosyl rutin production.","description":"In this paper, the cgt gene encoding cyclodextrin glycosyltransferase (CGTase) from <i>Bacillus stearothermophilus</i> was cloned into pWB980 plasmid for extracellular expression in <i>Bacillus subtilis</i> SCK6. Through adding a six-histidine affinity tag fused to the C-terminus, the recombinant CGTase could be purified by nickel ion affinity chromatography, and its molecular weight was approximately 76 kDa on SDS-PAGE. Then, the enzymatic properties were determined, and results were as follows: the optimum temperature and pH were identified as 40 ℃ and pH 5.0, respectively. CGTase had good tolerance to metal ions of Mn<sup>2+</sup>, Ca<sup>2+</sup>, and Mg<sup>2+</sup>. The enzyme activity was activated by Na<sup>+</sup>, Al<sup>3+</sup>, Fe<sup>3+</sup>, and Ni<sup>+</sup>, and it was r","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Mar","modification":"2026-06-02T19:25:49.88Z","creation":"2025-04-04T20:40:54.342Z"},"accession":"S-EPMC9925633","cross_references":{"pubmed":["36798855"],"doi":["10.1007/s13205-023-03510-5"]}}