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Braz J Microbiol ; 55(1): 169-177, 2024 Mar.
Article in English | MEDLINE | ID: mdl-38019411

ABSTRACT

Amphiphilic protein has lipophilic and hydrophilic domains, displaying the potential for development as a biosurfactant. The polyhydroxyalkanoate (PHA) surface binding protein derived from Bacillus is a type of protein that has not been studied for its emulsifying properties. In this study, PHA granule-associated protein (PhaP), PHA regulatory protein (PhaQ), and PHA synthase subunit (PhaR) derived from an alkali-tolerant PHA-producing Bacillus cereus HBL-AI were found and heterologously expressed in E. coli and purified to investigate their application as biosurfactants. It showed that the emulsification ability and stability of three amphiphilic proteins were higher than those of widely used chemical surfactants in diesel oil, vegetable oil, and lubricating oil. In particular, the PhaQ protein studied for the first time can form a stable emulsion layer in vegetable oil at a lower concentration (50 µg/mL), which greatly reduced the amount of protein used in emulsification. This clearly demonstrated that the PHA-binding protein of HBL-AI can be well applied as an environmentally friendly biosurfactants.


Subject(s)
Bacillus , Polyhydroxyalkanoates , Polyhydroxyalkanoates/metabolism , Bacillus/genetics , Bacillus/metabolism , Carrier Proteins/genetics , Carrier Proteins/metabolism , Membrane Proteins , Surface-Active Agents/metabolism , Escherichia coli/metabolism , Bacterial Proteins/genetics , Bacterial Proteins/metabolism
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