Microbial transformation of tectoridin from Pueraria flos by Lactobacillus and bifidobacteria

Ying Liu; Gang Cheng; Ting Han; Hong Yang; SA Ibrahim; Wen Huang

doi:10.1016/j.foodchem.2011.08.050

Microbial transformation of tectoridin from Pueraria flos by Lactobacillus and bifidobacteria

Ying Liu
, Gang Cheng
, Ting Han
, Hong Yang
, SA Ibrahim
, Wen Huang

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Tectoridin could be hydrolyzed to tectorigenin by β-glucosidase- producing intestinal bacteria. In this study, nine strains of Lactobacillus and bifidobacteria were screened for high levels of β-glucosidase activity. We investigated their ability to transform tectoridin from Pueraria flos to tectorigenin. Lactobacillus reuteri DSM20016 showed the highest cell-envelope associated β-glucosidase activity, whereas the intracellular β-glucosidase activity from Bifidobacterium adolescentis ATCC15703 was higher than the other screened bacterial strains. L. reuteri DSM20016, Lactobacillus rhamnosus GGB41031 and B. adolescentis ATCC15703 showed high bioconversion rate of tectoridin. L. reuteri DSM20016 showed the highest bioconversion efficiency of tectoridin, 100% tectoridin was hydrolyzed and there was an approximate 185-fold increase in the concentration of tectorigenin after 24 h. The present study suggests that L. reuteri DSM20016, L. rhamnosus GGB41031 and B. adolescentis ATCC15703 have great potential for converting tectoridin from Pueraria flos to more bioactive tectorigenin. © 2011 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	149-154
Number of pages	6
Journal	Food Chemistry
Volume	131
Issue number	1
DOIs	https://doi.org/10.1016/j.foodchem.2011.08.050
State	Published - Mar 1 2012

Keywords

β-Glucosidase activity
Bifidobacteria
Bioconversion
Lactobacillus
Tectoridin
Tectorigenin

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10.1016/j.foodchem.2011.08.050

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title = "Microbial transformation of tectoridin from Pueraria flos by Lactobacillus and bifidobacteria",

abstract = "Tectoridin could be hydrolyzed to tectorigenin by β-glucosidase- producing intestinal bacteria. In this study, nine strains of Lactobacillus and bifidobacteria were screened for high levels of β-glucosidase activity. We investigated their ability to transform tectoridin from Pueraria flos to tectorigenin. Lactobacillus reuteri DSM20016 showed the highest cell-envelope associated β-glucosidase activity, whereas the intracellular β-glucosidase activity from Bifidobacterium adolescentis ATCC15703 was higher than the other screened bacterial strains. L. reuteri DSM20016, Lactobacillus rhamnosus GGB41031 and B. adolescentis ATCC15703 showed high bioconversion rate of tectoridin. L. reuteri DSM20016 showed the highest bioconversion efficiency of tectoridin, 100\% tectoridin was hydrolyzed and there was an approximate 185-fold increase in the concentration of tectorigenin after 24 h. The present study suggests that L. reuteri DSM20016, L. rhamnosus GGB41031 and B. adolescentis ATCC15703 have great potential for converting tectoridin from Pueraria flos to more bioactive tectorigenin. {\textcopyright} 2011 Elsevier Ltd. All rights reserved.",

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AU - Ibrahim, SA

AU - Huang, Wen

PY - 2012/3/1

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Microbial transformation of tectoridin from Pueraria flos by Lactobacillus and bifidobacteria

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Keywords

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