19 March 2013 Purification of soyasaponin -β-galactosidase from Aspergillus sp.39
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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.
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Jing Tian, Ping Zhao, Longquan Xu, Xu Fei, 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); doi: 10.1117/12.2019642; https://doi.org/10.1117/12.2019642
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