Enzyme Design by Chemical Modification of Papain Lysine

Author

Xue, Yong ; Li, Shu-Bai ; Zhang, Hai-Tao ; Nie, Hua-Li ; Zhu, Li-Min ; Branford-White, Christopher J.

Author_Institution

Coll. of Chem., Chem. Eng. & Biotechnol., Donghua Univ., Shanghai, China

fYear

2009

fDate

11-13 June 2009

Firstpage

1

Lastpage

4

Abstract

Papain (EC 3.4.22.2) has been chemically modified using two reagents including different anhydrides of maleic and poly-maleic acids. The average ratio of modified-NH₂ was tested by trinitrobenzenesulfonic acid (TNBS) method. The native and modified papain were purified by dialysis and their structures were characterized by FTIR. The factor related with the activity of the modified papain, such as temperature, pH value and kinetic constant were studied and compared with the native papain. The resultant papain had its optimum pH shifted from 6.0 to 9.0. Compared with native papain, the thermal stability and the resistance to alkali of modified enzyme were improved considerably. Among the enzyme, poly-maleic anhydride modified enzyme was found to be the best in catalytic efficiency.

Keywords

Fourier transform spectrometers; bio-optics; biochemistry; biological techniques; catalysis; enzymes; infrared spectrometers; molecular biophysics; thermal stability; FTIR spectrometry; catalytic efficiency; enzyme design; papain lysine chemical modification; poly-maleic anhydride modified enzyme; thermal stability; trinitrobenzenesulfonic acid method; Amino acids; Biochemistry; Biotechnology; Chemical analysis; Chemical engineering; Educational institutions; Kinetic theory; Temperature; Thermal resistance; Thermal stability;

fLanguage

English

Publisher

ieee

Conference_Titel

Bioinformatics and Biomedical Engineering , 2009. ICBBE 2009. 3rd International Conference on

Conference_Location

Beijing

Print_ISBN

978-1-4244-2901-1

Electronic_ISBN

978-1-4244-2902-8

Type

conf

DOI

10.1109/ICBBE.2009.5162789

Filename

5162789