{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang J"],"funding":["National Natural Science Foundation of China"],"pagination":["3487"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10528286"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(18)"],"pubmed_abstract":["Malto-oligosaccharides (MOSs) from starch conversion is advantageous for food and pharmaceutical applications. In this study, an efficient malto-oligosaccharide-forming α-amylase AmyCf was identified from myxobacter <i>Cystobacter</i> sp. strain CF23. AmyCf is composed of 417 amino acids with N-terminal 41 amino acids as the signal peptide, and conserved glycoside hydrolase family 13 (GH13) catalytic module and predicted C-terminal domain with β-sheet structure are also identified. Phylogenetic and functional analysis demonstrated that AmyCf is a novel member of GH13_6 subfamily. The special activity of AmyCf toward soluble starch and raw wheat starch is 9249 U/mg and 11 U/mg, respectively. AmyCf has broad substrate specificity toward different types of starches without requiring Ca<sup>2+"],"journal":["Foods (Basel, Switzerland)"],"pubmed_title":["Identification and Characterization of Novel Malto-Oligosaccharide-Forming Amylase AmyCf from <i>Cystobacter</i> sp. Strain CF23."],"pmcid":["PMC10528286"],"funding_grant_id":["32070027","32270066","32170123","32270060"],"pubmed_authors":["Wang P","Li Z","Lei J","Huang Y","Cui Z","Zhang L","Luo X","Zhan L","Wang J","Ye X","Zhong L"],"additional_accession":[]},"is_claimable":false,"name":"Identification and Characterization of Novel Malto-Oligosaccharide-Forming Amylase AmyCf from <i>Cystobacter</i> sp. Strain CF23.","description":"Malto-oligosaccharides (MOSs) from starch conversion is advantageous for food and pharmaceutical applications. In this study, an efficient malto-oligosaccharide-forming α-amylase AmyCf was identified from myxobacter <i>Cystobacter</i> sp. strain CF23. AmyCf is composed of 417 amino acids with N-terminal 41 amino acids as the signal peptide, and conserved glycoside hydrolase family 13 (GH13) catalytic module and predicted C-terminal domain with β-sheet structure are also identified. Phylogenetic and functional analysis demonstrated that AmyCf is a novel member of GH13_6 subfamily. The special activity of AmyCf toward soluble starch and raw wheat starch is 9249 U/mg and 11 U/mg, respectively. AmyCf has broad substrate specificity toward different types of starches without requiring Ca<sup>2+","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Sep","modification":"2026-04-08T13:29:32.18Z","creation":"2025-02-19T04:08:18.164Z"},"accession":"S-EPMC10528286","cross_references":{"pubmed":["37761198"],"doi":["10.3390/foods12183487"]}}