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Enhancement of the Tyrosinase Inhibitory Activity of Mori Cortex Radicis Extract by Biotransformation UsingLeuconostoc paramesenteroidesPR
Author(s) -
Jung Sung Kim,
Hyun Ju You,
Hye Yoon Kang,
Geun Eog Ji
Publication year - 2012
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.111002
Subject(s) - tyrosinase , biotransformation , glycosidic bond , chemistry , enzyme , hydrolysis , biochemistry , stereochemistry
Mori Cortex Radicis (MCR), the root bark of Morus alba L., consists of various phytochemicals and exhibits a strong inhibitory effect on tyrosinase. To enhance the tyrosinase inhibitory activity of MCR extract without further purification of bioactive compounds, whole MCR extract was biotransformed with crude enzyme extract from a selected lactic acid bacterium, Leuconostoc paramesenteroides PR (LP). Mulberroside A (MA), a major stilbene glucoside of MCR, contains two β-glucosyl residues at the C3 and C4' positions of oxyresveratrol (OXY). The crude enzyme of LP hydrolyzed the two glycosidic bonds of MA effectively, and 97.1% of MA was biotransformed into OXY within 2 h. Commercial almond β-glucosidase hydrolyzed only one site of the two glycosidic bonds of MA, and 68.7% of MA was biotransformed to OXY-glucoside. The tyrosinase inhibitory activity of the crude extract of MCR was increased approximately 6.5-fold by biotransformation using LP, and the IC(50) value of the transformed MCR was 3.7 µg/mL.

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