Roberta Teixeira Polez, Thamiris Voltarelli Ferracini, Samuel Filipe Cardoso de Paula, Rachel Passos de Oliveira Santos, André L M Porto, Elisabete Frollini
{"title":"纤维素己酸酯、苯甲酸酯和混合酯的合成:探索它们作为酶固定平台的潜力。","authors":"Roberta Teixeira Polez, Thamiris Voltarelli Ferracini, Samuel Filipe Cardoso de Paula, Rachel Passos de Oliveira Santos, André L M Porto, Elisabete Frollini","doi":"10.1002/mabi.202500221","DOIUrl":null,"url":null,"abstract":"<p><p>This study utilizes cellulose sourced from cotton linters to synthesize cellulose esters-hexanoate, benzoate, and mixed hexanoate-benzoate-with varying degrees of substitution (DS). These esters create electrospun mats that immobilize Pseudomonas fluorescens lipase (PFL), also in a configuration where an intermediate layer is added to a mat using an airbrush filled with PFL, covered by a third layer of electrospun mat. PFL-incorporated spheres are produced from cellulose ester solutions. DS, acyl chain length, and electrospinning parameters influence the morphology of the electrospun mat, which consists of nanofibers and ultrafine fibers. The PFL-incorporated mats show poor catalytic activity in resolving racemic (R,S)-2-chloro-1-phenylethanol, likely due to enzyme deactivation from high-voltage electrospinning. In contrast, mat-layered structures with PFL immobilized without voltage nearly doubled the conversion rate, although it was still lower than that of free enzymes. Spheres enhanced biocatalysis, achieving a 40% conversion rate with 94% enantiomeric purity while retaining 76% of their initial conversion rate in a subsequent reaction cycle. This research is the first to explore cellulose esters for the enzymatic immobilization of PFL to resolve a racemic mixture. The findings may enable PFL-incorporated structures in broader biocatalysis applications; the materials created may be tested to support the immobilization of other enzymes.</p>","PeriodicalId":18103,"journal":{"name":"Macromolecular bioscience","volume":" ","pages":"e00221"},"PeriodicalIF":4.1000,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Synthesis of Cellulose Hexanoate, Benzoate, and Mixed Esters: Exploring Their Potential as Enzyme Immobilization Platforms.\",\"authors\":\"Roberta Teixeira Polez, Thamiris Voltarelli Ferracini, Samuel Filipe Cardoso de Paula, Rachel Passos de Oliveira Santos, André L M Porto, Elisabete Frollini\",\"doi\":\"10.1002/mabi.202500221\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>This study utilizes cellulose sourced from cotton linters to synthesize cellulose esters-hexanoate, benzoate, and mixed hexanoate-benzoate-with varying degrees of substitution (DS). These esters create electrospun mats that immobilize Pseudomonas fluorescens lipase (PFL), also in a configuration where an intermediate layer is added to a mat using an airbrush filled with PFL, covered by a third layer of electrospun mat. PFL-incorporated spheres are produced from cellulose ester solutions. DS, acyl chain length, and electrospinning parameters influence the morphology of the electrospun mat, which consists of nanofibers and ultrafine fibers. The PFL-incorporated mats show poor catalytic activity in resolving racemic (R,S)-2-chloro-1-phenylethanol, likely due to enzyme deactivation from high-voltage electrospinning. In contrast, mat-layered structures with PFL immobilized without voltage nearly doubled the conversion rate, although it was still lower than that of free enzymes. Spheres enhanced biocatalysis, achieving a 40% conversion rate with 94% enantiomeric purity while retaining 76% of their initial conversion rate in a subsequent reaction cycle. This research is the first to explore cellulose esters for the enzymatic immobilization of PFL to resolve a racemic mixture. 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Synthesis of Cellulose Hexanoate, Benzoate, and Mixed Esters: Exploring Their Potential as Enzyme Immobilization Platforms.
This study utilizes cellulose sourced from cotton linters to synthesize cellulose esters-hexanoate, benzoate, and mixed hexanoate-benzoate-with varying degrees of substitution (DS). These esters create electrospun mats that immobilize Pseudomonas fluorescens lipase (PFL), also in a configuration where an intermediate layer is added to a mat using an airbrush filled with PFL, covered by a third layer of electrospun mat. PFL-incorporated spheres are produced from cellulose ester solutions. DS, acyl chain length, and electrospinning parameters influence the morphology of the electrospun mat, which consists of nanofibers and ultrafine fibers. The PFL-incorporated mats show poor catalytic activity in resolving racemic (R,S)-2-chloro-1-phenylethanol, likely due to enzyme deactivation from high-voltage electrospinning. In contrast, mat-layered structures with PFL immobilized without voltage nearly doubled the conversion rate, although it was still lower than that of free enzymes. Spheres enhanced biocatalysis, achieving a 40% conversion rate with 94% enantiomeric purity while retaining 76% of their initial conversion rate in a subsequent reaction cycle. This research is the first to explore cellulose esters for the enzymatic immobilization of PFL to resolve a racemic mixture. The findings may enable PFL-incorporated structures in broader biocatalysis applications; the materials created may be tested to support the immobilization of other enzymes.
期刊介绍:
Macromolecular Bioscience is a leading journal at the intersection of polymer and materials sciences with life science and medicine. With an Impact Factor of 2.895 (2018 Journal Impact Factor, Journal Citation Reports (Clarivate Analytics, 2019)), it is currently ranked among the top biomaterials and polymer journals.
Macromolecular Bioscience offers an attractive mixture of high-quality Reviews, Feature Articles, Communications, and Full Papers.
With average reviewing times below 30 days, publication times of 2.5 months and listing in all major indices, including Medline, Macromolecular Bioscience is the journal of choice for your best contributions at the intersection of polymer and life sciences.