We are analyzing https://link.springer.com/protocol/10.1007/978-1-4939-8672-9_18.

Title:
Lipase-Catalyzed Acetylation and Esterification of Bile Acids | SpringerLink
Description:
In this chapter we describe the application of lipases as catalysts in reactions on a relevant family of steroids: the bile acids. Twenty three monoacetyl, diacetyl, and ester derivatives of deoxycholic, chenodeoxycholic, lithocholic, and cholic acids, 15 of them new...
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Keywords {🔍}

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Topics {✒️}

month download article/chapter 20β-hemisuccinyloxy-5αh-pregnan-3 p-toluenesulfonic acid/methanol lipase-catalysed regioselective deacetylation lipase-catalyzed regioselective preparation privacy choices/manage cookies device instant download editor information editors acetylated ester products laboratorio de biocatálisis garcía liñares fatty acid esters lipase-catalysed deacetylation lipase-catalyzed acetylation lipase-catalysed preparation lipase-catalyzed preparation low-cost lipase transbuccal drug delivery bruttomesso ac springer nature biologically active esters 6α-ethylchenodeoxycholic acid european economic area nucleophile/substrate ratio traditional synthetic procedures vitro cytotoxic activity pro-apoptotic process human cell lines chemical permeation enhancers transdermal penetration principles vitamin-b6 group bactericide lapyrium chloride enzyme-catalysed transformations ent-kaurane diterpenoids lipase-catalyzed synthesis cholic acid showed enzyme-catalyzed preparation enzyme/substrate ratio journal finder publish lipase-catalyzed acylation bile acid amphiphiles tunable head groups comparative spectroscopic analysis conditions privacy policy short-step synthesis multiple methacrylate groups accepting optional cookies cholic acid derivatives bile acids protocol bile acid derivatives

Schema {🗺️}

ScholarlyArticle:
      headline:Lipase-Catalyzed Acetylation and Esterification of Bile Acids
      pageEnd:350
      pageStart:337
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-4939-8672-9.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Lipases and Phospholipases
         isbn:
            978-1-4939-8672-9
            978-1-4939-8671-2
         type:Book
      publisher:
         name:Springer New York
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Alicia Baldessari
            affiliation:
                  name:Universidad de Buenos Aires
                  address:
                     name:Facultad de Ciencias Exactas y Naturales, Laboratorio de Biocatálisis, Departamento de Quimica Orgánica y UMYMFOR, Universidad de Buenos Aires, Buenos Aires, Argentina
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Guadalupe García Liñares
            affiliation:
                  name:Universidad de Buenos Aires
                  address:
                     name:Facultad de Ciencias Exactas y Naturales, Laboratorio de Biocatálisis, Departamento de Quimica Orgánica y UMYMFOR, Universidad de Buenos Aires, Buenos Aires, Argentina
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Lipases, Acetylation, Esterification, Alcoholysis, Bile acids
      description:In this chapter we describe the application of lipases as catalysts in reactions on a relevant family of steroids: the bile acids. Twenty three monoacetyl, diacetyl, and ester derivatives of deoxycholic, chenodeoxycholic, lithocholic, and cholic acids, 15 of them new compounds, were obtained through lipase-catalyzed acetylation, esterification, and alcoholysis reactions in very good to excellent yield and a highly regioselective way. Among them, acetylated ester products, in which the lipase catalyzed both reactions in one pot, were obtained. The influence of various reaction parameters in the enzymatic reactions, such as enzyme source, nucleophile/substrate ratio, enzyme/substrate ratio, solvent, and temperature, was studied. Some of the reported products are novel, and it is not possible to obtain them satisfactorily by following traditional synthetic procedures. Due to its singular structure containing three hydroxyl groups, cholic acid showed a different behavior in the enzymatic reactions, from that observed for the other three bile acids studied. In order to shed light to different behaviors of bile acids in the enzymatic reactions, molecular modeling was applied to substrates and some derivatives.
      datePublished:2018
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Book:
      name:Lipases and Phospholipases
      isbn:
         978-1-4939-8672-9
         978-1-4939-8671-2
Organization:
      name:Springer New York
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Universidad de Buenos Aires
      address:
         name:Facultad de Ciencias Exactas y Naturales, Laboratorio de Biocatálisis, Departamento de Quimica Orgánica y UMYMFOR, Universidad de Buenos Aires, Buenos Aires, Argentina
         type:PostalAddress
      name:Universidad de Buenos Aires
      address:
         name:Facultad de Ciencias Exactas y Naturales, Laboratorio de Biocatálisis, Departamento de Quimica Orgánica y UMYMFOR, Universidad de Buenos Aires, Buenos Aires, Argentina
         type:PostalAddress
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      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Alicia Baldessari
      affiliation:
            name:Universidad de Buenos Aires
            address:
               name:Facultad de Ciencias Exactas y Naturales, Laboratorio de Biocatálisis, Departamento de Quimica Orgánica y UMYMFOR, Universidad de Buenos Aires, Buenos Aires, Argentina
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Guadalupe García Liñares
      affiliation:
            name:Universidad de Buenos Aires
            address:
               name:Facultad de Ciencias Exactas y Naturales, Laboratorio de Biocatálisis, Departamento de Quimica Orgánica y UMYMFOR, Universidad de Buenos Aires, Buenos Aires, Argentina
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Facultad de Ciencias Exactas y Naturales, Laboratorio de Biocatálisis, Departamento de Quimica Orgánica y UMYMFOR, Universidad de Buenos Aires, Buenos Aires, Argentina
      name:Facultad de Ciencias Exactas y Naturales, Laboratorio de Biocatálisis, Departamento de Quimica Orgánica y UMYMFOR, Universidad de Buenos Aires, Buenos Aires, Argentina
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