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A comparison of changes in transformation of isoflavones in soymilk using varying concentrations of exogenous and probiotic-derived endogenous ß-glucosidases

journal contribution
posted on 2024-11-01, 12:37 authored by Daniel Otieno, Nagendra Shah
To compare endogenous and exogenous beta-glucosidases for the hydrolysis of the predominant isoflavone glucosides in soymilk in order to improve the biological activity. Beta-glucosidase activity of probiotic organisms, including Bifidobacterium animalis ssp. lactis Bb12, Lactobacillus acidophilus ATCC 4461 and Lactobacillus casei 2607 in soymilk, was evaluated and was related to the increase in the concentration of isoflavone aglycones during fermentation. The concentrations of isoflavone compounds in soymilk were monitored using a Varian model HPLC with an Amperometric electrochemical detector. The aglycone composition, also known as aglycone equivalent ratio, has been considered to be important for the delivery of health benefits of isoflavones, and was monitored during the fermentation of soymilk. Comparison of the hydrolytic effectiveness of both exogenous and endogenous enzyme during 4-h incubation in soymilk was conducted using the Otieno-Shah (O-S) index. Results showed that exogenous enzyme exhibited faster rate of isoflavone glucoside hydrolysis than that by endogenous enzyme. Highest O-S indices were obtained after 4, 3 and 2 h of incubation with enzyme solution having beta-glucosidase activity of 0.288 U ml(-1), 0.359 U ml(-1) and 0.575 U ml(-1), resulting into aglycone concentration increments of 5.87-, 6.07- and 5.94-fold, respectively. Conversely, aglycone concentration in the soymilk with B. animalis ssp. lactis Bb12, L. casei 2607 and L. acidophilus 4461 increased by 3.43-, 2.72- and 3.03-fold, respectively, after 4 h of fermentation at 37 degrees C.

History

Related Materials

  1. 1.
    DOI - Is published in 10.1111/j.1365-2672.2006.03245
  2. 2.
    ISSN - Is published in 13645072

Journal

Journal of Applied Microbiology

Volume

103

Start page

601

End page

612

Total pages

12

Publisher

Wiley-Blackwell

Place published

United Kingdom

Language

English

Copyright

©2007 The Authors

Former Identifier

2006038698

Esploro creation date

2020-06-22

Fedora creation date

2013-01-06