인문학
사회과학
자연과학
공학
의약학
농수해양학
예술체육학
복합학
DBpia AI
AI 에이전트
AI 아이디어
AI 리더
AI 뷰어
Citeasy
크롬 서지관리 다운로드
지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
Abstract Objectives The primary aim of this study is to immobilize glucose oxidase (GOX) as a model enzyme using a simple and efficient method without the use of any toxic chemicals. This will enable the multiple reusability of GOX, thereby reducing the process cost. Furthermore, the objective is to determine the kinetic, optimum pH, and temperature parameters in comparison to soluble GOX. Methods For immobilization, GOX at a concentration of 5 mg/mL was mixed with an equal volume of hypol prepolymer in a beaker. Immobilization was achieved by the formation of amide bonds between –NH 2 groups on the enzyme surface and the prepolymer. The activities of polyurethane foam (PUF)-immobilized and soluble GOX were monitored using horse radish peroxidase enzyme as a second enzyme. 2,2′-Azino-bis-3-ethylbenzothiazoline-6-sulfonic acid radical ABTS + generated as a result of the enzymatic reactions was detected at 420 nm. Results The kinetic parameters for soluble GOX were Km=9.39 ± 1.13 mM and V max =9.14 ± 0.45 A.U sec −1 × 10 −4 , while for PUF-immobilized GOX Km=10.04 ± 1.30 mM and V max =9.09 ± 0.49 A.U sec −1 × 10 −4 . PUF-immobilized GOX displayed high performance during reuse experiments. PUF-immobilization led to the activity at higher temperatures and over a wide pH range compared to its soluble counterpart. Conclusions GOX was successfully immobilized for the first time using PUF. This technique can be used in the healthcare and food sectors as well as in biosensor applications. In the future, when successfully applied to many enzymes of industrial value, it could offer significant advantages.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
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