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Enantioselective oligomerization of alpha-hydroxy carboxylic acids and alpha-amino acids

a technology which is applied in the field of enantioselective oligomerization of alpha-hydroxy carboxylic acids and alpha-amino acids, can solve the problems of not being able to efficiently utilize feed, unable to provide protein or amino acids to animals for absorption, and not being able to protect animals

Inactive Publication Date: 2007-08-23
NOVUS INTERNATIONAL INC
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Unfortunately, these proteins and α-amino acids can be subjected to extensive degradation in the rumen by ruminal microorganisms, thereby rendering the protein or amino acid unavailable to the animal for absorption.
This is not a very efficient utilization of the feed, which is especially problematic in animals having increased nutritional requirements such as lactating dairy cows and fast growing animals such as beef cattle.
Underheating the protein resulted in no protection while overheating the protein resulted in the degradation of important essential amino acids.
Many of such supplements are difficult to provide, however, due to being soluble in water which causes the supplements to dissolve before they can be ingested.
However, the difficulty involved in the analysis of higher order, water insoluble oligomers, presents a unique challenge to biochromatography.

Method used

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  • Enantioselective oligomerization of alpha-hydroxy carboxylic acids and alpha-amino acids
  • Enantioselective oligomerization of alpha-hydroxy carboxylic acids and alpha-amino acids
  • Enantioselective oligomerization of alpha-hydroxy carboxylic acids and alpha-amino acids

Examples

Experimental program
Comparison scheme
Effect test

example 1

Synthesis of Methionine Oligomers and HMB-Methionine Co-Oligomers

[0180] This example demonstrates the enzymatic synthesis of oligomers comprising methionine and co-oligomers comprising HMB-methionine, as well as their characterization using reverse-phase HPLC and matrix assisted laser desorption ionization-time of flight mass spectroscopy (MALDI-TOF MS) analysis.

Co-Oligomerization

[0181] In a first synthesis, the experiment was generally conducted in accordance with reaction conditions for the papain-catalyzed oligomerization of methionine analogs as described by Arai et al. in Agric. Biol. Chem., 43(5), 1069-1074 (1979). The oligomerization comprised forming a reaction mixture at a temperature of 37° C. consisting of nanopure filtered water (10 mL) containing HMB ethyl ester (0.7 M) and methionine ethyl ester (0.7 M) along with L-cysteine (0.1 M), EDTA (10 mM), sodium citrate (1M) and 1% papain (by weight of the monomer) at a pH of 5.5. The mixture was allowed to incubate for 24...

example 2

Oligomerization and Co-Oligomerization of Lysine and HMB

[0195] This example demonstrates four alternative procedures for the enzymatic synthesis of oligomers comprising lysine and co-oligomers comprising HMB-lysine. The experiment was designed to compare three novel synthesis procedures to that of Puigserver et. al.1 who reported a procedure for papain catalyzed polymerization of lysine.

[0196] In general, protease-catalyzed synthesis of water insoluble amino acid oligomers in aqueous media is driven by precipitation. The synthesis of water soluble oligomers of amino acids, such as lysine can be controlled only in mixed phase systems where the equilibria is shifted in favor of the synthesis of polypeptides due to enhanced partitioning of peptide in the organic phase. Puigserver et. al. reported a procedure for papain catalyzed polymerization of lysine which involved the binding of papain to modified PEG (MW 2000 or 5000). The bound enzyme was then used to synthesize poly lysine in ...

example 3

[0201] HMB-methionine and HMB-lysine co-polymers were synthesized enzymatically through a papain-catalyzed reaction along with poly-methionine and poly-lysine (as controls) as described in Examples 1 and 2. The biological release of the amino acids from the oligomers was examined using several digestive enzymes including pepsin, trypsin, chymotrypsin, intestinal peptidase and carboxypeptidase. The oligomers were dissolved at 10 mg / mL in 0.15 HCl (pH 2.5) or 50 mM KPO4 (pH 7.5). Samples (0.5 mL) were incubated with 10 units of each enzyme for 2 hours at 37° C. The extent of digestion was quantified by measurement of newly released amino groups and their reaction with o-Phthalaldehyde (OPA) and 2,4,6-trinitrobenzene sulfonic acid (TNBSA). Acid hydrolysis was prepared by complete hydrolysis of 10 mg / mL polymers in 6 M HCl for 24 hours at 110° C. Results are summarized below in Table 3.

[0202] Results show that HMB-methionine and HMB-lysine can be hydrolyzed by strong acid and heat. HMB...

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Abstract

An enzymatic synthesis and composition of oligomers and co-oligomers comprised of α-hydroxy carboxylic acids and α-amino acids or peptides is disclosed. In a preferred embodiment, a α-hydroxy carboxylic acid with a specific chiral configuration is linked by an amide linkage to a α-amino acid specific with a specific chiral configuration or linked by an amide linkage to a peptide made up of α-amino acid monomers having identical chiral configurations. Proteolytic enzymes catalyze oligomerization of the α-hydroxy carboxylic acid and α-amino acid. The degree and distribution of oligomerization varies upon the type and concentrations of different reaction mixtures utilized and upon the length of allowed reaction time. The resultant oligomers may be provided to animals such as ruminants as bioavailable amino acid supplements that are resistant to degradation in the rumen and other animals such as swine, poultry and aquatic animals.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application is a divisional application of U.S. patent application Ser. No. 10 / 136,974, filed May 2, 2002, which claims priority from U.S. Provisional Application Serial No. 60 / 288,196, filed May 2, 2001, and as a continuation-in-part of U.S. patent application Ser. No. 09 / 699,946, filed Oct. 30, 2000, which claims priority from U.S. Provisional Application Serial No. 60 / 162,725, filed Oct. 29, 1999 (now abandoned). The entire texts of U.S. Provisional Application Serial No. 60 / 288,196, U.S. patent application Ser. Nos. 09 / 699,946 and 10 / 136,974, and U.S. Provisional Application Serial No. 60 / 288,196 are hereby incorporated herein by reference.BACKGROUND OF THE INVENTION [0002] The present invention relates to a process for the enantioselective preparation of oligomers consisting of α-amino acid isomers and co-oligomers consisting of α-hydroxy carboxylic acid isomers and α-amino acid isomers. The present invention also relates to c...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A23K1/165C12P21/06C12P7/62A23K1/16A23K1/18C07K2/00C07K7/06C12P21/00
CPCA23K1/1609A23K1/1631A23K1/1634A23K1/1653C12P21/00A23K1/1833A23K1/188C07K2/00C07K7/06A23K1/1813A23K20/105A23K20/147A23K20/142A23K20/189A23K50/00A23K50/10A23K50/80
Inventor LORBERT, STEPHEN J.SCHASTEEN, CHARLES S.NAM, PAUL K.S.FORCINITI, DANIELRAJESH, MATHUR P.KAPILA, SHUBHENDER
Owner NOVUS INTERNATIONAL INC
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