TY - JOUR
T1 - Activity adaptability of a DhHP-6 peroxidase-mimic in wide pH and temperature ranges and solvent media
AU - Yan, Jiaqing
AU - Li, Zhengqiang
AU - Liu, Min
AU - Sun, Xiaoli
AU - Ma, Li
AU - Wang, Zhi
AU - Zhao, Zijian
AU - Huang, Xuri
AU - Yuan, Long
N1 - Publisher Copyright:
© 2020 The Royal Society of Chemistry.
PY - 2020/3/21
Y1 - 2020/3/21
N2 - Separating the active units while maintaining the majority of the functions of enzymes seems to be a paradox and therefore challenging, not to mention also improving the adaptability to harsh conditions simultaneously. In this paper, we demonstrate that a well-designed hexapeptide molecule, deuterohemin-β-Ala-His-Thr-Val-Glu-Lys (DhHP-6), adapted from cytochrome c, shows superior peroxidase activity over a wide pH and temperature range. The activity of DhHP-6 was first assessed via three substrates (i.e., 2,2′azinodi(3-ethylbenzthiazoline)-6-sulfonate (ABTS), 1,2,3-trihydroxybenzene (THB) and phenol) with reference to the classically studied examples microperoxidase (MP-11) and horseradish peroxidase (HRP). The environmental adaptability was assessed via three factors: pH, temperature, and the polarity of solvents. In the phenol substrate model reaction, DhHP-6 shows superior specific activity (749.73 U mg-1) and adaptability compared to HRP (311.32 U mg-1). Under the optimum solvent conditions (15% methanol by volume ratio), the enzymatic efficiency (Vm/Km) of DhHP-6 reached 27.9 × 10-3 s-1, 16-times higher than that of HRP (1.81 × 10-3 s-1). The methanol concentration dependent electron paramagnetic spectra show an axial-promoted intermediate process for the phenol catalytic reaction. This work provides a protocol and feasible methodology for the design and fabrication of natural enzyme mimicking small molecules that maintain most of their native activity for better biocatalytic applications in organic pollutant remediation and other related processes.
AB - Separating the active units while maintaining the majority of the functions of enzymes seems to be a paradox and therefore challenging, not to mention also improving the adaptability to harsh conditions simultaneously. In this paper, we demonstrate that a well-designed hexapeptide molecule, deuterohemin-β-Ala-His-Thr-Val-Glu-Lys (DhHP-6), adapted from cytochrome c, shows superior peroxidase activity over a wide pH and temperature range. The activity of DhHP-6 was first assessed via three substrates (i.e., 2,2′azinodi(3-ethylbenzthiazoline)-6-sulfonate (ABTS), 1,2,3-trihydroxybenzene (THB) and phenol) with reference to the classically studied examples microperoxidase (MP-11) and horseradish peroxidase (HRP). The environmental adaptability was assessed via three factors: pH, temperature, and the polarity of solvents. In the phenol substrate model reaction, DhHP-6 shows superior specific activity (749.73 U mg-1) and adaptability compared to HRP (311.32 U mg-1). Under the optimum solvent conditions (15% methanol by volume ratio), the enzymatic efficiency (Vm/Km) of DhHP-6 reached 27.9 × 10-3 s-1, 16-times higher than that of HRP (1.81 × 10-3 s-1). The methanol concentration dependent electron paramagnetic spectra show an axial-promoted intermediate process for the phenol catalytic reaction. This work provides a protocol and feasible methodology for the design and fabrication of natural enzyme mimicking small molecules that maintain most of their native activity for better biocatalytic applications in organic pollutant remediation and other related processes.
UR - http://www.scopus.com/inward/record.url?scp=85082759418&partnerID=8YFLogxK
U2 - 10.1039/c9cy01855g
DO - 10.1039/c9cy01855g
M3 - Article
AN - SCOPUS:85082759418
SN - 2044-4753
VL - 10
SP - 1848
EP - 1857
JO - Catalysis Science and Technology
JF - Catalysis Science and Technology
IS - 6
ER -