Purification of soyasaponin -β-galactosidase from Aspergillus sp.39

Jing Tian; Ping Zhao; Longquan Xu; Xu Fei; Yi Wang

doi:10.1117/12.2019642

19 March 2013 Purification of soyasaponin -β-galactosidase from Aspergillus sp.39

Jing Tian, Ping Zhao, Longquan Xu, Xu Fei, Yi Wang

Proceedings Volume 8762, PIAGENG 2013: Intelligent Information, Control, and Communication Technology for Agricultural Engineering; 87621F (2013) https://doi.org/10.1117/12.2019642
Event: Third International Conference on Photonics and Image in Agriculture Engineering (PIAGENG 2013), 2013, Sanya, China

Abstract

In order to increase physiological activity of soyasaponin, enzyme hydrolysis of soyasaponin was studied. The enzyme which hydrolyzes soyasaponin to lower sugar soyasaponin was obtained from Aspergillus sp.39s. And it was purified by the method of biologic chromatography system. The method of SDS-polyacrylamide gel electrophoresis was used to determine the molecular weight of the enzyme produced by Aspergillus sp.39s. The molecular weight was about 50 kDa. The optimum pH and temperature of soyasaponin-β-galactosidase produced from sp.39s was 5.0 and 40°C respectively. Soyasaponin-β-galactosidase was comparatively stable in the pH range from 3.0 to 7.0 and in the temperature range from 20°C to 60°C.

Citation Download Citation

Jing Tian, Ping Zhao, Longquan Xu, Xu Fei, and Yi Wang "Purification of soyasaponin -β-galactosidase from Aspergillus sp.39", Proc. SPIE 8762, PIAGENG 2013: Intelligent Information, Control, and Communication Technology for Agricultural Engineering, 87621F (19 March 2013); https://doi.org/10.1117/12.2019642

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