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Production of β-Glucosidase and Hydrolysis of Isoflavone Phytoestrogens by Lactobacillus acidophilus, Bifidobacterium lactis, and Lactobacillus casei in Soymilk

Donkor, Osaana N and Shah, Nagendra P (2008) Production of β-Glucosidase and Hydrolysis of Isoflavone Phytoestrogens by Lactobacillus acidophilus, Bifidobacterium lactis, and Lactobacillus casei in Soymilk. Journal of Food Science, 73 (1). M15-M20. ISSN 0022-1147

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Abstract

The study determined β-glucosidase activity of commercial probiotic organisms for hydrolysis of isoflavone to aglycones in fermenting soymilk. Soymilkmade with soy protein isolate (SPI)was fermented with Lactobacillus acidophilus LAFTI� L10, Bifidobacterium lactis LAFTI� B94, and Lactobacillus casei LAFTI� L26 at 37 ◦C for 48 h and the fermented soymilkwas stored for 28 d at 4 ◦C. β-Glucosidase activity of organisms was determined using ρ-nitrophenyl β-D-glucopyranoside as a substrate and the hydrolysis of isoflavone glycosides to aglycones by these organisms was carried out. The highest level of growth occurred at 12 h for L. casei L26, 24 h for B. lactis B94, and 36 h for L. acidophilus L10 during fermentation in soymilk. Survival after storage at 4 ◦C for 28 d was 20%, 15%, and 11% greater (P < 0.05) than initial cell counts, respectively. All the bacteria produced β-glucosidase, which hydrolyzed isoflavone β-glycosides to isoflavone aglycones. The decrease in the concentration of β-glycosides and the increase in the concentration of aglyconeswere significant (P <0.05) in the fermented soymilk. Increased isoflavone aglycone content in fermented soymilk is likely to improve the biological functionality of soymilk.

Item Type: Article
Uncontrolled Keywords: ResPubID15474. aglycone, β-glucosidase, isoflavones, soy protein isolate, viability
Subjects: Faculty/School/Research Centre/Department > Institute for Sustainability and Innovation (ISI)
FOR Classification > 0908 Food Sciences
SEO Classification > 8602 Dairy Products
Depositing User: VUIR
Date Deposited: 21 Sep 2011 23:01
Last Modified: 21 Sep 2011 23:01
URI: http://vuir.vu.edu.au/id/eprint/3628
DOI: 10.1111/j.1750-3841.2007.00547.x
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Citations in Scopus: 51 - View on Scopus

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