Bacillus phenylalanine dehydrogenase produced in Escherichia coli. Its purification and application to L-phenylalanine synthesis.
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چکیده
منابع مشابه
Affinity Purification and Characterization of Recombinant Bacillus sphaericus Phenylalanine Dehydrogenase Produced by pET Expression Vector System
Cloning and expression of the L-phenylalanine dehydrogenase gene, from B. sphaericus in E. coli were done. The gene was cloned in the vector pET16b and transformed into E. coli BL21 (DE3). The functional form of the L-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, Re...
متن کاملaffinity purification and characterization of recombinant bacillus sphaericus phenylalanine dehydrogenase produced by pet expression vector system
cloning and expression of the l-phenylalanine dehydrogenase gene, from b. sphaericus in e. coli were done. the gene was cloned in the vector pet16b and transformed into e. coli bl21 (de3). the functional form of the l-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, re...
متن کاملGenetic engineering of Escherichia coli to improve L-phenylalanine production
BACKGROUND L-phenylalanine (L-Phe) is an essential amino acid for mammals and applications expand into human health and nutritional products. In this study, a system level engineering was conducted to enhance L-Phe biosynthesis in Escherichia coli. RESULTS We inactivated the PTS system and recruited glucose uptake via combinatorial modulation of galP and glk to increase PEP supply in the Xllp...
متن کاملRapid One-Step Separation and Purification of Recombinant Phenylalanine Dehydrogenase in Aqueous Two-Phase Systems
Background: Phenylalanine dehydrogenase (PheDH EC 1.4.1.20) is a NAD+-dependent enzyme that performs the reversible oxidative deamination of L-phenylalanine to phenylpyruvate. It plays an important role in detection and screening of phenylketonuria (PKU) diseases and production of chiral intermediates as well. The main goal of this study was to find a simple and rapid alternative method for pur...
متن کاملEnzymic synthesis of N-acetyl-L-phenylalanine in Escherichia coli K12.
1. Cell-free extracts of Escherichia coli K12 catalyse the synthesis of N-acetyl-l-phenylalanine from acetyl-CoA and l-phenylalanine. 2. The acetyl-CoA-l-phenylalanine alpha-N-acetyltransferase was purified 160-fold from cell-free extracts. 3. The enzyme has a pH optimum of 8 and catalyses the acetylation of l-phenylalanine. Other l-amino acids such as histidine and alanine are acetylated at sl...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1987
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.51.2621