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State of Pepsin and Acidic Protease in Solid Phase System and the Factors Increasing Their Destabilization
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作者 H. T. Hasanov A. H. Boboev +1 位作者 A. H. Hasanov M. M. Rahimov 《Journal of Food Science and Engineering》 2011年第4期303-312,共10页
The adsorption state and catalytic properties of pepsin and acidic protease from microorganisms Asp. awamori and Asp. oryzae were studied in solid phase system (in presence of sorsilen, DEAE- and CM-cellulose). Acco... The adsorption state and catalytic properties of pepsin and acidic protease from microorganisms Asp. awamori and Asp. oryzae were studied in solid phase system (in presence of sorsilen, DEAE- and CM-cellulose). According to the results, adsorption capacity and catalytic activity of enzymes depend on the physical nature of surface groups of the solid phase. Changing the stability of enzymes in the system with solid phase is observed even the adsorption bond is less stable (in the case of DEAE- and CM-cellulose in acidic media). Injection to the medium ethanol, surfactants, sodium chloride and changing the temperature of the incubation medium could prevent the negative effects of the solid phases. When sorsilen is used as solid phase, pepsin and acidic protease from Asp. awamori suffer from high surface inactivation. Various surfactants influence adsorption state of enzymes differently. Non-ionic surfactants (Triton X-100) prevent adsorption and restore catalytic properties of enzymes. 展开更多
关键词 PEPSIN acid proteinase Asp. awamori Asp. oryzae sorsilen adsorption state inactivation regulation.
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