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Application of α-amylase as a novel biodemulsifier for destabilizing amphiphilic polymer-flooding produced liquid treatment
- Jiang, Jiatong, Wu, Hairong, Lu, Yao, Ma, Tao, Li, Zhe, Xu, Derong, Kang, Wanli, Bai, Baojun
- Bioresource technology 2018 v.259 pp. 349-356
- alpha-amylase, ambient temperature, emulsions, hydrolysis, industry, liquids, molecular weight, petroleum, polymers, salinity, surface tension, viscosity, zeta potential
- The performance and de-emulsification mechanism of α-amylase, a novel environmental friendly biodemulsifier in petroleum industry, was investigated at room temperature. The effects of α-amylase on the viscosity of amphiphilic polymer solution and de-emulsification rate were studied by changing the concentration of α-amylase, temperature and salinity. Polymer molecular weight, Zeta potential, interfacial film strength and interfacial tension were measured to investigate the de-emulsification mechanism of α-amylase. The results show that α-amylase is an efficient biodemulsifier to increase the de-emulsification rate of amphiphilic polymer emulsions. Hydrolysis of α-amylase to amphiphilic polymers destroys the structure of the amphiphilic polymer, thereby reduces the viscosity and the interfacial film strength of the system. Once de-emulsification is completed, the lower layer, i.e. the emulsified layer, will be clear. Thus, α-amylase can be applied as an effective de-emulsifier for amphiphilic polymer-stabilized O/W emulsion.