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Owing to its broad substrate specificity, it has attracted growing interest in biotechnology, food processing, pharmaceuticals, and natural product modification. Fungal and bacterial \u03b1-L-rhamnosidases show diversity in molecular architecture, catalytic efficiency, thermostability, and pH tolerance, while sharing a conserved inverting mechanism mediated by acidic residues within the GH78 and GH106 families. Structural studies reveal catalytic cores, substrate recognition motifs, and aromatic residues involved in rhamnose binding. These enzymes enable the production of bioactive compounds such as prunin, isoquercitrin, quercetin, hesperetin, icariin, and myricetin. Recent advances in computational design, protein engineering, and directed evolution have improved enzyme performance. This review summarizes the current knowledge of microbial \u03b1-L-rhamnosidases, emphasizing their sources, biochemical characteristics, substrate specificity, structural organization, catalytic mechanisms, therapeutic relevance, and recent advances in protein engineering.<\/jats:p>","DOI":"10.1021\/acs.jafc.6c08020","type":"journal-article","created":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T02:07:33Z","timestamp":1788314853000},"page":"27346-27370","source":"Crossref","is-referenced-by-count":0,"title":["Structural and\nFunctional Perspectives of \u03b1-L-Rhamnosidase\nin Glycoside Biotransformation, Therapeutic Applications, and Enzyme\nEngineering"],"prefix":"10.1021","volume":"74","author":[{"given":"Kunwar","family":"Vishal","sequence":"first","affiliation":[{"name":"Chhatrapati Shahu Ji Maharaj University , , , ,","place":["Kanpur, Uttar Pradesh, India, 208024"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vinita","family":"Yadav","sequence":"additional","affiliation":[{"name":"Chhatrapati Shahu Ji Maharaj University , , , ,","place":["Kanpur, Uttar Pradesh, India, 208024"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0026-1684","authenticated-orcid":true,"given":"Pramod K.","family":"Yadav","sequence":"additional","affiliation":[{"name":"Chhatrapati Shahu Ji Maharaj University , , , ,","place":["Kanpur, Uttar Pradesh, India, 208024"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,28]]},"reference":[{"key":"2026090917070012400_cit1","volume-title":"Glycosidases:\nfunctions, families and folds","author":"Ko\u0308tzler","year":"2014"},{"issue":"D1","key":"2026090917070012400_cit2","doi-asserted-by":"publisher","first-page":"D571","DOI":"10.1093\/nar\/gkab1045","article-title":"The carbohydrate-active\nenzyme database: functions\nand literature","volume":"50","author":"Drula","year":"2022","journal-title":"Nucleic Acids Res."},{"issue":"7","key":"2026090917070012400_cit3","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1007\/s11274-023-03638-9","article-title":"\u03b1-L-rhamnosidase:\nProduction, properties, and applications","volume":"39","author":"Pan","year":"2023","journal-title":"World\nJ. Microbiol. Biotechnol."},{"issue":"2","key":"2026090917070012400_cit4","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1007\/s13205-018-1139-9","article-title":"Characterization of a glycoside hydrolase\nfamily 78 \u03b1-l-rhamnosidase from Bacteroides thetaiotaomicron\nVPI-5482 and identification of functional residues","volume":"8","author":"Li","year":"2018","journal-title":"3 Biotechnol."},{"key":"2026090917070012400_cit5","doi-asserted-by":"publisher","first-page":"108189","DOI":"10.1016\/j.abb.2019.108189","article-title":"The crystal\nstructure and insight into the substrate specificity of the \u03b1-L\nrhamnosidase RHA-P from Novosphingobium sp. PP1Y","volume":"679","author":"Terry","year":"2020","journal-title":"Arch. Biochem. 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