Abstract
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.
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Acknowledgements
The authors would like to thank faculty and Head, Department of Biotechnology and Food Technology, Punjabi University, Patiala for providing help and guidance for smooth succession of this work. The authors would also like to thank Director, Principal, Mata Gujri College Fatehgarh Sahib, Punjab, India for providing financial support and state-of-art research laboratory.
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Dr JS conceived the idea and supervised the work while SG carried out experiments and wrote the manuscript reviewed by Dr MT and Dr JS.
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Singh, J., Goyal, S. & Tripathi, M.K. α-Amylase inhibitory, antioxidant and emulsification potential of glycoproteinaceous bioactive molecule from Lactobacillus delbrueckii. J Food Sci Technol 61, 459–470 (2024). https://doi.org/10.1007/s13197-023-05851-8
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DOI: https://doi.org/10.1007/s13197-023-05851-8