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
d-Allulose is one of the rare monosaccharides and is considered as a safe ingredient in foods. It can be enzymatically produced from d-fructose by the enzyme d-allulose 3-epimerase. More stable enzymes can operate effectively for longer durations, reducing the need for frequent replacements and thereby lowering costs. In addition, the preparation of the recombinant Arthrobacter globiformis M30 (AgDAE) enzyme requires heat treatment at 60-70 °C to remove host cell debris and potential microbial contaminants. Therefore, to address the need for more thermostable enzymes in d-allulose production, we aimed to create thermostable mutants of AgDAE using the protein engineering method. We cloned d-allulose identified from A. globiformis M30 and, using sequence homology, we constructed thermostable mutants by protein engineering. Each effect of the five mutations used was independent and additive. By integrating positive mutations, we succeeded in the construction of a chimeric enzyme exhibiting hyperthermostability without loss of enzymatic activity. The constructed chimera mutant was highly functional above 95 °C and remained stable under 80 °C. Our approach using structural information for the chimeric construction experiments also suggested that incorporating mutations from other homologous enzymes can impart advantages in enzymes in a simple and effective manner.
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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