Improved viability of spray-dried Lactobacillus bulgaricus sp1.1 embedded in acidic-basic proteins treated with transglutaminase

•Electrostatic attraction of basic protein to cells increased survival rates of spray-dried bacteria.•Transglutaminase treated basic and acidic proteins retained 84% viable bacteria after drying.•Close connection between protein and cells can increase the protective efficiency. Spray drying is a fas...

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Bibliographic Details
Published in:Food chemistry 2019-05, Vol.281, p.204-212
Main Authors: Gong, Pimin, Di, Wei, Yi, Huaxi, Sun, Jialei, Zhang, Lanwei, Han, Xue
Format: Article
Language:English
Subjects:
Cross-linked proteins
Culture Media - chemistry
Desiccation - methods
Hydrogen-Ion Concentration
Lactic acid bacteria
Lactobacillus delbrueckii
Microbial Viability
Milk basic protein
Milk Proteins - chemistry
Powders
Soybean Proteins - chemistry
Spectroscopy, Fourier Transform Infrared
Spray drying
Transglutaminase
Transglutaminases - metabolism
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Summary:•Electrostatic attraction of basic protein to cells increased survival rates of spray-dried bacteria.•Transglutaminase treated basic and acidic proteins retained 84% viable bacteria after drying.•Close connection between protein and cells can increase the protective efficiency. Spray drying is a fast and low-cost method of drying lactic acid bacteria, but it features a low survival rate. A pre-treatment was designed to increase the survival by embedding bacteria in basic or acidic proteins with the principle of opposite charges attraction. Transglutaminase (TGase)-induced cross-linking then tightened the cell–protein complexes. The results showed that mixing of basic proteins with acidic proteins and TGase treatment increased the survival rates of spray-dried Lactobacillus bulgaricus sp1.1. 84.78% of cells in the TGase-treated milk basic protein (MBP)-soy protein isolate (SPI) bacterial solution remained after drying. Positively charged MBP adhered to more bacteria (negative charge) and formed tight closed loop-shaped complexes with SPI (negative charge) by electrostatic attraction, and TGase enhanced this attraction by strengthening of the hydrogen, CO and CN bonds and exposing the inner α-helix. Imbedding bacteria in TGase-treated acidic–basic protein can increase efficiency of the current formulation.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2018.12.095