Global InformationInulinase information
| Inulinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.7 | ||||||||
| CAS no. | 9025-67-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Inulinase (EC 3.2.1.7 and EC 3.2.1.8, inulase, endoinulinase, endo-inulinase, exoinulinase, 2,1-β-D-fructan fructanohydrolase) is an enzyme with systematic name 1-β-D-fructan fructanohydrolase.[1][2]
It catalyses the reaction:
- Endohydrolysis of (2→1)-β-D-fructosidic linkages in inulin
Inulinase has 2 EC numbers of 3.2.1.7,[3] and 3.2.1.8,[2] for endo- and -exo inulinases, respectively. This classifies it as a hydrolase, specifically a glycosylase of glycosidic nature capable of hydrolyzing O- and S- glycosyl. Due to its chemical reactions, the food industry uses this enzyme to create high fructose syrup. It can be extracted from many tuber vegetables, such as Jerusalem artichoke, dahlia, and chicory.[4]
- ^ Adams M, Richtmyer NK, Hudson CS (1943). "Some enzymes present in highly purified invertase preparations; a contribution to the study of fructofuranosidases, galactosidases, glucosidases and mannosidases". J. Am. Chem. Soc. 65 (7): 1369–1380. doi:10.1021/ja01247a029.
- ^ a b Liu Y, Zhou SH, Cheng YR, Chi Z, Chi ZM, Liu GL (2016). "Synergistic effect between the recombinant exo-inulinase and endo-inulinase on inulin hydrolysis". Journal of Molecular Catalysis B: Enzymatic. 128: 27–38. doi:10.1016/j.molcatb.2016.03.005. ISSN 1381-1177.
- ^ "Information on EC 3.2.1.7 - inulinase".
- ^ Jain SC, Jain PC, Kango N (January 2012). "Production of inulinase from Kluyveromyces marxianus using dahlia tuber extract". Brazilian Journal of Microbiology. 43 (1): 62–69. doi:10.1590/S1517-83822012000100007. PMC 3768966. PMID 24031804.