Enzymatic synthesis ofN-acyl-l-amino acids in a glycerol-water system using acylase I from pig kidney

2002 ◽  
Vol 79 (1) ◽  
pp. 41-46 ◽  
Author(s):  
Eiko Wada ◽  
Masato Handa ◽  
Koreyoshi Imamura ◽  
Takaharu Sakiyama ◽  
Shuji Adachi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis ◽  
Water System ◽  
Glycerol Water ◽  
Pig Kidney ◽  
Acylase I

Enzymatic Synthesis of 15N-L-aspartic Acid Using Recombinant Aspartase from Escherichia Coli K12

2008 ◽  
Vol 59 (11) ◽  
Author(s):  
Iulia Lupan ◽  
Sergiu Chira ◽  
Maria Chiriac ◽  
Nicolae Palibroda ◽  
Octavian Popescu
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Enzymatic Synthesis ◽  
Large Scale ◽  
Recombinant Dna ◽  
Industrial Enzymes ◽  
Recombinant Dna Technology ◽  
Bacterial Fermentation ◽  
Natural Protein ◽  
Novel Method

Amino acids are obtained by bacterial fermentation, extraction from natural protein or enzymatic synthesis from specific substrates. With the introduction of recombinant DNA technology, it has become possible to apply more rational approaches to enzymatic synthesis of amino acids. Aspartase (L-aspartate ammonia-lyase) catalyzes the reversible deamination of L-aspartic acid to yield fumaric acid and ammonia. It is one of the most important industrial enzymes used to produce L-aspartic acid on a large scale. Here we described a novel method for [15N] L-aspartic synthesis from fumarate and ammonia (15NH4Cl) using a recombinant aspartase.

Characterization of an isozyme of S-adenosylmethionine synthetase from rat liver

1984 ◽  
Vol 62 (5) ◽  
pp. 276-279 ◽  
Author(s):  
C. H. Lin ◽  
W. Chung ◽  
K. P. Strickland ◽  
A. J. Hudson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Adenosylmethionine Synthetase ◽  
Cellulose Column

An isozyme of S-adenosylmethionine synthetase has been purified to homogeneity by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and gel filtration on a Sephadex G-200 column. The purified enzyme is very unstable and has a molecular weight of 120 000 consisting of two identical subunits. Amino acid analysis on the purified enzyme showed glycine, glutamate, and aspartate to be the most abundant and the aromatic amino acids to be the least abundant. It possesses tripolyphosphatase activity which can be stimulated five to six times by S-adenosylmethionine (20–40 μM). The findings support the conclusion that an enzyme-bound tripolyphosphate is an obligatory intermediate in the enzymatic synthesis of S-adenosylmethionine from ATP and methionine.

Enzymatic Synthesis of α-Butylglucoside in a Biphasic Butanol-Water System Using the α-Transglucosidase from Aspergillus niger

1999 ◽  
pp. 291-296 ◽  
Author(s):  
Marie-Pierre Bousquet ◽  
René-Marc Willemot ◽  
Pierre F. Monsan ◽  
François Paul ◽  
Emmanuel Boures
Keyword(s):  
Aspergillus Niger ◽  
Enzymatic Synthesis ◽  
Water System

Least cost diets to reduce nitrogen excretion by growing and finishing pigs

1995 ◽  
Vol 1995 ◽  
pp. 36-36
Author(s):  
R.M. Kay ◽  
P.A. Lee
Keyword(s):  
Amino Acids ◽  
Protein Quality ◽  
Water System ◽  
Nitrogen Retention ◽  
Essential Amino Acids ◽  
Nitrogen Excretion ◽  
Finishing Pigs ◽  
Ideal Protein ◽  
The Uk ◽  
Feeding Diets

In the UK, pollution of the water system with nitrate nitrogen leaching from the soil is seen as a major problem and farm animal effluents have been identified as a major source of nitrate pollution. It would, therefore, be beneficial to the livestock producer and to the environment if the nitrogen excretion from animals could be kept to a minimum. To limit the excretion of nitrogen by the pig, it is necessary to supply amino acids in the diet in better agreement with its dietary requirements. This could be achieved either by feeding diets according to the pig's requirements based on age and/or weight (phase feeding) or by improving protein quality. The best protein quality would be that which has the same balance of essential amino acids (EAA) with respect to lysine as that required by the pig, i.e. ideal protein. Diets formulated on the basis of total dietary EAA on an ideal protein basis, using crystalline EAA, could enable lower crude protein (CP) diets to be offered whilst maintaining nitrogen retention (NR). An alternative approach to formulating diets would be to base the formulations on either: 1) currently available, commercial database values for ileal digestible EAA values of ingredients to achieve diets as close to ideal protein as possible but within least cost formulation constraints; or 2) ingredients limited simply to cereals and pulses and supplemented with crystalline EAA to formulate as close to ideal protein as possible. The object of the present experiment was to evaluate diets, formulated on this basis, in terms of nitrogen intake (NI), excretion (NE) and retention (NR) in pigs using balance studies.

Multi-Enzymatic Synthesis of Optically Pure β-Hydroxy α-Amino Acids

2014 ◽  
Vol 357 (4) ◽  
pp. 767-774 ◽  
Author(s):  
Makoto Hibi ◽  
Takuya Kasahara ◽  
Takashi Kawashima ◽  
Hiroko Yajima ◽  
Shoko Kozono ◽  
...  
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis ◽  
Optically Pure

Distribution, industrial applications, and enzymatic synthesis of d-amino acids

2015 ◽  
Vol 99 (8) ◽  
pp. 3341-3349 ◽  
Author(s):  
Xiuzhen Gao ◽  
Qinyuan Ma ◽  
Hailiang Zhu
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis ◽  
Industrial Applications

ChemInform Abstract: Enzymatic Synthesis of Unnatural Amino Acids

ChemInform ◽  
2009 ◽  
Vol 40 (52) ◽  
Author(s):  
Mari Hara Yasuda ◽  
Makoto Ueda ◽  
Kazuya Okano ◽  
Hisaaki Mihara ◽  
Nobuyoshi Esaki
Keyword(s):  
Amino Acids ◽  
Enzymatic Synthesis ◽  
Unnatural Amino Acids

scholarly journals Stabilization of Curcumin by Complexation with Divalent Cations in Glycerol/Water System

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
Bachar Zebib ◽  
Zéphirin Mouloungui ◽  
Virginie Noirot
Keyword(s):  
Divalent Cations ◽  
Water System ◽  
Mechanical Mixture ◽  
Divalent Ions ◽  
Glycerol Water ◽  
Water Solvent ◽  
Metal Metal ◽  
Sulfate Salts ◽  
In Vitro Stability

The purpose of present study was to stabilize curcumin food pigment by its complexation with divalent ions like , in “green media” and evaluate its stability in vitro compared to curcumin alone. The curcumin complexes were prepared by mechanical mixture of curcumin and sulfate salts of each metal (metal : curcumin 1/1mol) into unconventional and nontoxic glycerol/water solvent. Two stoichiometry of complex were obtained, 1 : 1 and 1 : 2 (metal/curcumin), respectively. On evaluation of in vitro stability, all complexes were found to provide a higher stability from curcumin alone.

Human acetyl-CoA:glucosamine-6-phosphate N-acetyltransferase 1 has a relaxed donor specificity and transfers acyl groups up to four carbons in length

2016 ◽  
Vol 94 (2) ◽  
pp. 197-204 ◽  
Author(s):  
Inka Brockhausen ◽  
Dileep G. Nair ◽  
Min Chen ◽  
Xiaojing Yang ◽  
John S. Allingham ◽  
...  
Keyword(s):  
Amino Acids ◽  
Articular Cartilage ◽  
Enzymatic Synthesis ◽  
Biomedical Applications ◽  
Binding Pocket ◽  
Wild Type ◽  
Acetyl Coenzyme A ◽  
Site Specific ◽  
Acetyl Group

Glucosamine-6-phosphate N-acetyltransferase1 (GNA1) catalyses the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to glucosamine-6-phosphate (GlcN6P) to form N-acetylglucosamine-6-phosphate (GlcNAc6P), which is an essential intermediate in UDP-GlcNAc biosynthesis. An analog of GlcNAc, N-butyrylglucosamine (GlcNBu) has shown healing properties for bone and articular cartilage in animal models of arthritis. The goal of this work was to examine whether GNA1 has the ability to transfer a butyryl group from butyryl-CoA to GlcN6P to form GlcNBu6P, which can then be converted to GlcNBu. We developed fluorescent and radioactive assays and examined the donor specificity of human GNA1. Acetyl, propionyl, n-butyryl, and isobutyryl groups were all transferred to GlcN6P, but isovaleryl-CoA and decanoyl-CoA did not serve as donor substrates. Site-specific mutants were produced to examine the role of amino acids potentially affecting the size and properties of the AcCoA binding pocket. All of the wild type and mutant enzymes showed activities of both acetyl and butyryl transfer and can therefore be used for the enzymatic synthesis of GlcNBu for biomedical applications.

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