TY - JOUR
T1 - The functional emulsifying component of SL-bioemulsifier is an SDR family oxidoreductase protein
AU - Tao, Weiyi
AU - Li, Dongmei
AU - Lin, Junzhang
AU - Wang, Weidong
AU - Li, Shuang
N1 - Publisher Copyright:
© 2022 Elsevier B.V.
PY - 2022/10/5
Y1 - 2022/10/5
N2 - Hypothesis: Bioemulsifiers play an important role in microbial enhanced oil recovery (MEOR) due to their excellent emulsion stability. Different from biosurfactants, bioemulsifiers cannot significantly reduce the oil-water interfacial tension, and the mechanism through which they improve oil recovery remains poorly understood. It is helpful to study the mechanism by analyzing its functional emulsifying components of bioemulsifier. Experiments: In our previous work, the thermophilic strain Aeribacillus pallidus SL-1 efficiently degraded crude oil and insoluble polycyclic aromatic hydrocarbons (naphthalene and phenanthrene) with the help of a bioemulsifier. In this study, the glycoprotein SL-bioemulsifier was studied. Findings: The main functional emulsifying component was identified as a 26 kDa SDR family oxidoreductase protein, called E26. The recombinant E26 protein exhibited excellent emulsifying activity with different hydrophobic substrates, and stabilized the emulsions for a long time even at extreme pH, high salt concentrations and high temperatures. Notably, the emulsion formed by E26 protein was found to have a gel-like structure, facilitating the formation of an oil-water barrier to stabilize the emulsion. In addition, E26 protein effectively improved the surface wettability of calcite minerals in the oil-water system at a low concentration, which may play a role in the enhancement of oil recovery by bioemulsifiers.
AB - Hypothesis: Bioemulsifiers play an important role in microbial enhanced oil recovery (MEOR) due to their excellent emulsion stability. Different from biosurfactants, bioemulsifiers cannot significantly reduce the oil-water interfacial tension, and the mechanism through which they improve oil recovery remains poorly understood. It is helpful to study the mechanism by analyzing its functional emulsifying components of bioemulsifier. Experiments: In our previous work, the thermophilic strain Aeribacillus pallidus SL-1 efficiently degraded crude oil and insoluble polycyclic aromatic hydrocarbons (naphthalene and phenanthrene) with the help of a bioemulsifier. In this study, the glycoprotein SL-bioemulsifier was studied. Findings: The main functional emulsifying component was identified as a 26 kDa SDR family oxidoreductase protein, called E26. The recombinant E26 protein exhibited excellent emulsifying activity with different hydrophobic substrates, and stabilized the emulsions for a long time even at extreme pH, high salt concentrations and high temperatures. Notably, the emulsion formed by E26 protein was found to have a gel-like structure, facilitating the formation of an oil-water barrier to stabilize the emulsion. In addition, E26 protein effectively improved the surface wettability of calcite minerals in the oil-water system at a low concentration, which may play a role in the enhancement of oil recovery by bioemulsifiers.
KW - Bioemulsifier
KW - Emulsification
KW - MEOR
KW - SDR family oxidoreductase
KW - Wettability
UR - http://www.scopus.com/inward/record.url?scp=85133246960&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfa.2022.129590
DO - 10.1016/j.colsurfa.2022.129590
M3 - 文章
AN - SCOPUS:85133246960
SN - 0927-7757
VL - 650
JO - Colloids and Surfaces A: Physicochemical and Engineering Aspects
JF - Colloids and Surfaces A: Physicochemical and Engineering Aspects
M1 - 129590
ER -