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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제25권 제1호
- 발행연도
- 2015.1
- 수록면
- 33 - 43 (11page)
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초록· 키워드
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GAM-1 and GAM-2, two themostable glucoamylases from Aspergillus niger B-30, possess different molecular masses, glycosylation, and thermal stability. In the present study, the effects of additives on the thermal inactivation of GAM-1 and GAM-2 were investigated. The half-lives of GAM-1 and GAM-2 at 70ºC were 45 and 216 min, respectively. Data obtained from fluorescence spectroscopy, circular dichroism spectroscopy, UV absorption spectroscopy, and dynamic light scattering demonstrated that during the thermal inactivation progress, combined with the loss of the helical structure and a majority of the tertiary structure, tryptophan residues were partially exposed and further led to glucoamylases aggregating. The thermal stability of GAM-1 and GAM-2 was largely improved in the presence of sorbitol and trehalose. Results from spectroscopy and Native-PAGE confirmed that sorbitol and trehalose maintained the native state of glucoamylases and prevented their thermal aggregation. The loss of hydrophobic bonding and helical structure was responsible for the decrease of glucoamylase activity. Additionally, sorbitol and trehalose significantly increased the substrate affinity and catalytic efficiency of the two glucoamylases. Our results display an insight into the thermal inactivation of glucoamylases and provide an important base for industrial applications of the thermally stable glucoamylases.
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참고문헌 (23)
참고문헌 신청
Au sar SF / 2006 / Conformational stability and disassembly of Norwalk virus-like particles: effect of pH and temperature / J. Biol. Chem 281 : 19478 ~ 19488
Az izi A / 2011 / Effects of trehalose and sorbitol on the activity and structure of Pseudomonas cepacia lipase: spectroscopic insight / Int. J. Biol. Macromol 49 : 652 ~ 656
Ca ves MS / 2013 / Thermal inactivation of uricase (urate oxidase): mechanism and effects of additives / Biochemistry 52 : 497 ~ 507
Chi MC / 2012 / Sorbitol counteracts temperature and chemical-induced denaturation of a recombinant α-amylase from alkaliphilic Bacillus sp. TS-23 / J. Ind. Microbiol. Biote
Cui L / 2008 / Thermal stability and conformational changes of transglutaminase from a newly isolated Streptomyces hygroscopicus / Bioresour. Technol 99 : 3794 ~ 3800
Az izi A / 2011 / Effects of trehalose and sorbitol on the activity and structure of Pseudomonas cepacia lipase: spectroscopic insight / Int. J. Biol. Macromol 49 : 652 ~ 656
Ca ves MS / 2013 / Thermal inactivation of uricase (urate oxidase): mechanism and effects of additives / Biochemistry 52 : 497 ~ 507
Chi MC / 2012 / Sorbitol counteracts temperature and chemical-induced denaturation of a recombinant α-amylase from alkaliphilic Bacillus sp. TS-23 / J. Ind. Microbiol. Biote
Cui L / 2008 / Thermal stability and conformational changes of transglutaminase from a newly isolated Streptomyces hygroscopicus / Bioresour. Technol 99 : 3794 ~ 3800
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