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Development of an Improved Amino Ester Hydrolase for Continuous Reactive Crystallization of Beta-Lactam Antibiotics.- [electronic resources]
Development of an Improved Amino Ester Hydrolase for Continuous Reactive Crystallization of Beta-Lactam Antibiotics.- [electronic resources]
상세정보
- 자료유형
- 학위논문(국외)
- 자관 청구기호
- 기본표목-개인명
- 표제와 책임표시사항
- Development of an Improved Amino Ester Hydrolase for Continuous Reactive Crystallization of Beta-Lactam Antibiotics. - [electronic resources]
- 발행, 배포, 간사 사항
- 발행, 배포, 간사 사항
- 형태사항
- 306 p.
- 일반주기
- Source: Dissertations Abstracts International, Volume: 87-05, Section: B.
- 일반주기
- Advisor: Bommarius, Andreas S.;Grover, Martha A.
- 학위논문주기
- Thesis (Ph.D.)--Georgia Institute of Technology, 2023.
- 요약 등 주기
- 요약α-amino ester hydrolases (AEH) are a class of enzymes that are capable ofsynthesizing β-lactam antibiotics but are less studied than the industrially used penicillinG acylase (PGA). While both classes of enzymes synthesize a variety of β-lactamantibiotics, AEHs are promising candidates for enzymatic synthesis of cephalexin due totheir rapid kinetics and low pH optimum of activity but suffer from low thermostabilityand substrate inhibition. The goal of this thesis is to further develop a thermostable AEHoptimized for synthesis of β-lactam antibiotics and demonstrate a pilot plant for enzymaticreactive crystallization of both amoxicillin and cephalexin. While the pilot plant wasdesigned using PGA, further development of a stable AEH allows for future testing of AEHin a continuous reactive crystallization process. AEH kinetics were first characterized inbatch reactions, and a kinetic model was developed to describe cephalexin synthesis(Chapter 2). The relationships between AEH solution stability, oligomericity, anddeactivation were analyzed (Chapter 3). Using the kinetic model developed in Chapter 2,reactor designs were modelled and evaluated for AEH-catalyzed synthesis of cephalexin(Chapter 4). An improved AEH was developed to address low thermostability usingcomputationally guided rational design (Chapter 5). Using PGA, a pilot plant wasdeveloped for the enzymatic reactive crystallization of both cephalexin and amoxicillin(Chapter 6), and a novel magnetic separation system was developed to recycle immobilizedPGA and isolate pure crystalline API (Chapter 7).
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 부출표목-단체명
- 기본자료저록
- Dissertations Abstracts International. 87-05B.
- 전자적 위치 및 접속
- 원문정보보기
MARC
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■035 ▼a(MiAaPQ)GeorgiaTech75123
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a615.329
■090 ▼a전자자료
■1001 ▼aLagerman, Colton.
■24510▼aDevelopment of an Improved Amino Ester Hydrolase for Continuous Reactive Crystallization of Beta-Lactam Antibiotics.▼h[electronic resources]
■260 ▼a[S.l.]▼bGeorgia Institute of Technology. ▼c2023
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2023
■300 ▼a306 p.
■500 ▼aSource: Dissertations Abstracts International, Volume: 87-05, Section: B.
■500 ▼aAdvisor: Bommarius, Andreas S.;Grover, Martha A.
■5021 ▼aThesis (Ph.D.)--Georgia Institute of Technology, 2023.
■520 ▼aα-amino ester hydrolases (AEH) are a class of enzymes that are capable ofsynthesizing β-lactam antibiotics but are less studied than the industrially used penicillinG acylase (PGA). While both classes of enzymes synthesize a variety of β-lactamantibiotics, AEHs are promising candidates for enzymatic synthesis of cephalexin due totheir rapid kinetics and low pH optimum of activity but suffer from low thermostabilityand substrate inhibition. The goal of this thesis is to further develop a thermostable AEHoptimized for synthesis of β-lactam antibiotics and demonstrate a pilot plant for enzymaticreactive crystallization of both amoxicillin and cephalexin. While the pilot plant wasdesigned using PGA, further development of a stable AEH allows for future testing of AEHin a continuous reactive crystallization process. AEH kinetics were first characterized inbatch reactions, and a kinetic model was developed to describe cephalexin synthesis(Chapter 2). The relationships between AEH solution stability, oligomericity, anddeactivation were analyzed (Chapter 3). Using the kinetic model developed in Chapter 2,reactor designs were modelled and evaluated for AEH-catalyzed synthesis of cephalexin(Chapter 4). An improved AEH was developed to address low thermostability usingcomputationally guided rational design (Chapter 5). Using PGA, a pilot plant wasdeveloped for the enzymatic reactive crystallization of both cephalexin and amoxicillin(Chapter 6), and a novel magnetic separation system was developed to recycle immobilizedPGA and isolate pure crystalline API (Chapter 7).
■590 ▼aSchool code: 0078.
■650 4▼aAntibiotics.
■650 4▼aMagnetic fields.
■650 4▼aBinding sites.
■650 4▼aMicroscopy.
■650 4▼aCrystallization.
■650 4▼aDesign.
■650 4▼aKinetics.
■650 4▼aCrystals.
■650 4▼aPharmaceutical sciences.
■650 4▼aElectromagnetics.
■690 ▼a0389
■690 ▼a0572
■690 ▼a0607
■71020▼aGeorgia Institute of Technology.
■7730 ▼tDissertations Abstracts International▼g87-05B.
■790 ▼a0078
■791 ▼aPh.D.
■792 ▼a2023
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17360593▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
