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Substrates and enzyme activities related to biotransformation of resveratrol from phenylalanine by Alternaria sp. MG1.

Authors :
Zhang, Jinhua
Shi, Junling
Liu, Yanlin
Source :
Applied Microbiology & Biotechnology; Dec2013, Vol. 97 Issue 23, p9941-9954, 14p
Publication Year :
2013

Abstract

To identify the substrates and enzymes related to resveratrol biosynthesis in Alternaria sp. MG1, different substrates were used to produce resveratrol, and their influence on resveratrol production was analyzed using high performance liquid chromatography (HPLC). Formation of resveratrol and related intermediates was identified using mass spectrum. During the biotransformation, activities of related enzymes, including phenylalanine ammonia-lyase (PAL), trans-cinnamate 4-hydroxylase (C4H), and 4-coumarate-CoA ligase (4CL), were analyzed and tracked. The reaction system contained 100 mL 0.2 mol/L phosphate buffer (pH 6.5), 120 g/L Alternaria sp. MG1 cells, 0.1 g/L MgSO <subscript>4</subscript>, and 0.2 g/L CaSO <subscript>4</subscript> and different substrates according to the experimental design. The biotransformation was carried out for 21 h at 28 °C and 120 rpm. Resveratrol formation was identified when phenylalanine, tyrosine, cinnamic acid, and p-coumaric acid were separately used as the only substrate. Accumulation of cinnamic acid, p-coumaric acid, and resveratrol and the activities of PAL, C4H, and 4CL were identified and changed in different trends during transformation with phenylalanine as the only substrate. The addition of carbohydrates and the increase of phenylalanine concentration promoted resveratrol production and yielded the highest value (4.57 μg/L) when 2 g/L glucose, 1 g/L cyclodextrin, and phenylalanine (4.7 mmol/L) were used simultaneously. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
01757598
Volume :
97
Issue :
23
Database :
Complementary Index
Journal :
Applied Microbiology & Biotechnology
Publication Type :
Academic Journal
Accession number :
91857619
Full Text :
https://doi.org/10.1007/s00253-013-5212-3