<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang J</submitter><funding>National Natural Science Foundation of China</funding><pagination>3487</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10528286</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>12(18)</volume><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 &lt;i>Cystobacter&lt;/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&lt;sup>2+</pubmed_abstract><journal>Foods (Basel, Switzerland)</journal><pubmed_title>Identification and Characterization of Novel Malto-Oligosaccharide-Forming Amylase AmyCf from &lt;i>Cystobacter&lt;/i> sp. Strain CF23.</pubmed_title><pmcid>PMC10528286</pmcid><funding_grant_id>32070027</funding_grant_id><funding_grant_id>32270066</funding_grant_id><funding_grant_id>32170123</funding_grant_id><funding_grant_id>32270060</funding_grant_id><pubmed_authors>Wang P</pubmed_authors><pubmed_authors>Li Z</pubmed_authors><pubmed_authors>Lei J</pubmed_authors><pubmed_authors>Huang Y</pubmed_authors><pubmed_authors>Cui Z</pubmed_authors><pubmed_authors>Zhang L</pubmed_authors><pubmed_authors>Luo X</pubmed_authors><pubmed_authors>Zhan L</pubmed_authors><pubmed_authors>Wang J</pubmed_authors><pubmed_authors>Ye X</pubmed_authors><pubmed_authors>Zhong L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification and Characterization of Novel Malto-Oligosaccharide-Forming Amylase AmyCf from &lt;i>Cystobacter&lt;/i> sp. Strain CF23.</name><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 &lt;i>Cystobacter&lt;/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&lt;sup>2+</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Sep</publication><modification>2026-04-08T13:29:32.18Z</modification><creation>2025-02-19T04:08:18.164Z</creation></dates><accession>S-EPMC10528286</accession><cross_references><pubmed>37761198</pubmed><doi>10.3390/foods12183487</doi></cross_references></HashMap>