Chemoenzymatic synthesis and modification of well-defined macrolactonic sophorolipid (SLML) analogues via a series of successive regioselective de-esterification/transesterification reactions is investigated. Of the lipases screened, Candida antartica lipase-B (Novozyme-435) successfully deacylated the C60 acetoxy group of natural and peracylated SLMLs. Subsequent transesterification with acylating agents (esters of fatty acids) was successful only with the C-60 deacetylated natural SLML providing an avenue to well-defined analogues of varying amphilicity. The macrolactonic motif was essential for enzymatic recognition of the sophorose rings of these complex glycolipids. In the absence of the lactonic motif, the peracylated sophorose rings are not deacylated, rather the carboxyl end of the non-lactonic forms that was preferentially transesterified. All macrolactonic derivatives were characterized by IR, 1H, 13C, 1H-1H and 1H-13C NMR spectroscopy, as well as HRMS where applicable.
NMR spectroscopy, glycolipids, biosurfactant, sophorolipids, lipases, lactone, fatty acid esters
Publication DOI: 10.1016/j.tet.2017.02.043Journal NLM ID: 2984170RPublisher: Pergamon Press
Correspondence: Carr JA
; Carr JA
Institutions: Nazarbayev University, Department of Chemistry, Astana, Kazakhstan, University of California Irvine, Department of Chemistry, Irvine, USA
Methods: 13C NMR, 1H NMR, enzymatic digestion, HMBC, DEPT, COSY, HSQC, HRMS, FT-IR
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