Purification and characterisation of Aspergillus sojae naringinase

The production of prunin exhibiting markedly enhanced solubility with in vitro inhibition of HMG-CoA reductase

Hye Young Chang, Yoon Bok Lee, Hyun Ah Bae, Ji Young Huh, So Hyun Nam, Heon Soo Sohn, Hyong Joo Lee, Soo-Bok Lee

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Aspergillus sojae isolated from a traditional Korean fermented soybean product exhibited strong naringinase activity. The naringinase enzyme was purified and had a molecular weight of 70. kDa. The α- l-rhamnosidase activity of this enzyme was optimal at pH 6.0 and stable in the pH range of 5.5-8.0. The purified enzyme also had β- d-glucosidase activity, but the activity was relatively weak compared to the activity of the naringinase from Penicillium decumbens. The enzymatic bioconversion by A. sojae naringinase of naringin to prunin was efficiently performed with a 91% yield and a negligible amount of naringenin. The bioconversion was achieved by repetitive batch reactions with enzyme recycling. Prunin exhibited a markedly enhanced solubility compared to naringenin and naringin while maintaining the in vitro inhibition of HMG-CoA reductase. The results reported in this paper show that the naringinase produced by A. sojae will be useful in enhancing the potential bioavailability of naringin by efficiently converting it to prunin as a food component in citrus.

Original languageEnglish
Pages (from-to)234-241
Number of pages8
JournalFood Chemistry
Volume124
Issue number1
DOIs
Publication statusPublished - 2011 Jan 1

Fingerprint

naringinase
Hydroxymethylglutaryl CoA Reductases
Aspergillus
Solubility
Purification
solubility
naringin
Bioconversion
naringenin
Enzymes
biotransformation
Penicillium decumbens
alpha-L-rhamnosidase
enzymes
Glucosidases
soybean products
glucosidases
Citrus
Penicillium
Recycling

All Science Journal Classification (ASJC) codes

  • Food Science
  • Analytical Chemistry

Cite this

Chang, Hye Young ; Lee, Yoon Bok ; Bae, Hyun Ah ; Huh, Ji Young ; Nam, So Hyun ; Sohn, Heon Soo ; Lee, Hyong Joo ; Lee, Soo-Bok. / Purification and characterisation of Aspergillus sojae naringinase : The production of prunin exhibiting markedly enhanced solubility with in vitro inhibition of HMG-CoA reductase. In: Food Chemistry. 2011 ; Vol. 124, No. 1. pp. 234-241.
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abstract = "Aspergillus sojae isolated from a traditional Korean fermented soybean product exhibited strong naringinase activity. The naringinase enzyme was purified and had a molecular weight of 70. kDa. The α- l-rhamnosidase activity of this enzyme was optimal at pH 6.0 and stable in the pH range of 5.5-8.0. The purified enzyme also had β- d-glucosidase activity, but the activity was relatively weak compared to the activity of the naringinase from Penicillium decumbens. The enzymatic bioconversion by A. sojae naringinase of naringin to prunin was efficiently performed with a 91{\%} yield and a negligible amount of naringenin. The bioconversion was achieved by repetitive batch reactions with enzyme recycling. Prunin exhibited a markedly enhanced solubility compared to naringenin and naringin while maintaining the in vitro inhibition of HMG-CoA reductase. The results reported in this paper show that the naringinase produced by A. sojae will be useful in enhancing the potential bioavailability of naringin by efficiently converting it to prunin as a food component in citrus.",
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Purification and characterisation of Aspergillus sojae naringinase : The production of prunin exhibiting markedly enhanced solubility with in vitro inhibition of HMG-CoA reductase. / Chang, Hye Young; Lee, Yoon Bok; Bae, Hyun Ah; Huh, Ji Young; Nam, So Hyun; Sohn, Heon Soo; Lee, Hyong Joo; Lee, Soo-Bok.

In: Food Chemistry, Vol. 124, No. 1, 01.01.2011, p. 234-241.

Research output: Contribution to journalArticle

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