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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제26권 제7호
- 발행연도
- 2016.1
- 수록면
- 1,163 - 1,172 (10page)
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초록· 키워드
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The Ω-loop is a nonregular and flexible structure that plays an important role in molecular recognition, protein folding, and thermostability. In the present study, molecular dynamics simulation was carried out to assess the molecular stability and flexibility profile of the porcine trypsin structures. Two Ω-Loops (fragment 57–67 and fragment 78–91) were confirmed to represent the flexible region. Subsequently, glycosylation site-directed mutations (A73S, N84S, and R104S) were introduced within the Ω-loop region and its wing chain based on its potential N-glycosylation sites (Asn-Xaa-Ser/Thr consensus sequences) and structure information to improve the thermostability of trypsin. The result demonstrated that the halflife of the N84S mutant at 50°C increased by 177.89 min when compared with that of the wildtype enzyme. Furthermore, the significant increase in the thermal stability of the N84S mutant has also been proven by an increase in the Tm values determined by circular dichroism. Additionally, the optimum temperatures of the wild-type enzyme and the N84S mutant were 75°C and 80°C, respectively. In conclusion, we obtained the thermostability-improved enzyme N84S mutant, and the strategy used to design this mutant based on its structural information and N-linked glycosylation modification could be applied to engineer other enzymes to meet the needs of the biotechnological industry.
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참고문헌 (38)
참고문헌 신청
Badieyan S / 2012 / Study and design of stability in GH5 cellulases / Biotechnol. Bioeng 109:31~44
Bai Y / 1995 / Protein folding intermediates: native-state hydrogen exchange / Science 269:192~197
Çelik E / 2012 / Production of recombinant proteins by yeast cells / Biotechnol. Adv 30:1108~1118
Chen Y / 2015 / Improving the thermostability of β-lactoglobulin via glycation: the effect of sugar structures / Food Res. Int 69:106~113
Daly R / 2005 / Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production / J. Mol. Recognit 18:119~138
Bai Y / 1995 / Protein folding intermediates: native-state hydrogen exchange / Science 269:192~197
Çelik E / 2012 / Production of recombinant proteins by yeast cells / Biotechnol. Adv 30:1108~1118
Chen Y / 2015 / Improving the thermostability of β-lactoglobulin via glycation: the effect of sugar structures / Food Res. Int 69:106~113
Daly R / 2005 / Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production / J. Mol. Recognit 18:119~138
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