Earticle

현재 위치 Home

Abstracts for Colloquium

학생구두발표
Mass production of dihydroxybenzene glucosides by immobilization of amylosucrase

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2018 한국당과학회 연례학술대회 (2018.07)바로가기
  • 페이지
    pp.46-47
  • 저자
    Hun Sang Lee, Tae-Su Kim, Jae Kyung Sohng
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A346316

※ 원문제공기관과의 협약기간이 종료되어 열람이 제한될 수 있습니다.

원문정보

초록

영어
Dihydroxybenzenes exhibit biological functions such as anti- cancer, anti- inflammation, and antioxidants. They are also widely used in the cosmetics industry and as a treatment of skin related disease. In spite of these functions, they are easily oxidized by light in aqueous solutions and are limited by toxicity and side effects. The transglycosylation for these compounds have been shown to resolve these problems of solubility, stability and toxicity. Amylosucrase from Deinococcus geothermalis (DGAS) has been selected as the enzyme to be used for the transglycosylation. This enzyme is industrially useful because it supplies glucose using a relatively inexpensive donor substrate (sucrose). In this study, amylosucrase gene ( dgas) was codon optimized according to E. coli BL21 (DE3) codon usage. Sucrose was used as a source of glucose and it was used to produce three dihydroxybenzene (Hydroquinone, Resorcinol, Catechol) glucosides derivatives. Optimization of temperature, pH, donor (sucrose) and acceptor substrates concentrations increased glucoside derivative productivity. In addition, amyloglucosidase was used to reduced gluco-oligosaccharides and increased the production of mono-glucoside derivatives. Finally, the DgAS enzyme was immobilized on AMICOGEN LKZ118 beads. Immobilized enzyme could be used repeatedly up to 35 ~ 40 cycle on average. The percent yield of the total glycosides of hydroquinone and catechol varied from 85% to 90% until in immobilized system, however, in case of resorcinol the yield was in between 65% to 70%. It showed production of hydroquinone-mono-glucoside 13.3 g (35 cycle, 175mL), resorcinol-mono- glucoside 5.9 g ( 40 cycle, 200mL) and catechol-mono- glucoside 11.5g ( 40 cycle, 200mL) using a immobilized enzyme. The immobilized DgAS 1s cost reduction due to the separation and repeated use of the enzyme, to be effective for industrial application.

저자

  • Hun Sang Lee [ Department of Department of Bioscience and Eiocemical Engineering, SunMoon University ]
  • Tae-Su Kim [ Department of Department of Bioscience and Eiocemical Engineering, SunMoon University ]
  • Jae Kyung Sohng [ Department of Department of Bioscience and Eiocemical Engineering, SunMoon University ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    한국당과학회 [Korean Society for Glycoscience]
  • 설립연도
    2006
  • 분야
    의약학>약학
  • 소개
    본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.

간행물

  • 간행물명
    한국당과학회 학술대회
  • 간기
    연간
  • 수록기간
    2006~2022
  • 십진분류
    KDC 517 DDC 614

이 권호 내 다른 논문 / 한국당과학회 학술대회 2018 한국당과학회 연례학술대회

    피인용수 : 0건 (자료제공 : 네이버학술정보)

    함께 이용한 논문 이 논문을 다운로드한 분들이 이용한 다른 논문입니다.

      페이지 저장