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α-Amylase inhibitory, antioxidant and emulsification potential of glycoproteinaceous bioactive molecule from Lactobacillus delbrueckii
Jagdish Singh, Surbhi Goyal
α-Amylase inhibitory, antioxidant and emulsification potential of glycoproteinaceous bioactive molecule from Lactobacillus delbrueckii - p459-470
The bioactive components of microbial origin have been extensively applied to restrict the enormous enzyme-catalyzed processes. Hence, the present study was executed to explore the α -amylase inhibition (AAI) potential of glycoprotein isolated from Lactobacillus delbrueckii (LGp) to regulate in vitro starch hydrolysis. As a non-competitive inhibitor, the protein exhibited AAI (85%) with, IC50 135 ± 0.55 μg/mL. It was stable over a broad range of pH (3–11) and temperature (25–75 °C). Furthermore, LGp was significantly effective against amylase and starch from different sources. In addition, it also exhibited antioxidant and emulsifying potential. The UV, FT-IR and fluorescence analysis affirm the alterations in amylase molecular conformation after interaction with the LGp inhibitor. These results provide a substantial basis for the future use of LGp for controlled starch hydrolysis in vitro and as an antioxidant and emulsifying agent in the food industry.
Lactobacillus delbrueckii
Amylase activity
Enzyme inhibition
Antioxidant activity
α-Amylase inhibitory, antioxidant and emulsification potential of glycoproteinaceous bioactive molecule from Lactobacillus delbrueckii - p459-470
The bioactive components of microbial origin have been extensively applied to restrict the enormous enzyme-catalyzed processes. Hence, the present study was executed to explore the α -amylase inhibition (AAI) potential of glycoprotein isolated from Lactobacillus delbrueckii (LGp) to regulate in vitro starch hydrolysis. As a non-competitive inhibitor, the protein exhibited AAI (85%) with, IC50 135 ± 0.55 μg/mL. It was stable over a broad range of pH (3–11) and temperature (25–75 °C). Furthermore, LGp was significantly effective against amylase and starch from different sources. In addition, it also exhibited antioxidant and emulsifying potential. The UV, FT-IR and fluorescence analysis affirm the alterations in amylase molecular conformation after interaction with the LGp inhibitor. These results provide a substantial basis for the future use of LGp for controlled starch hydrolysis in vitro and as an antioxidant and emulsifying agent in the food industry.
Lactobacillus delbrueckii
Amylase activity
Enzyme inhibition
Antioxidant activity