Enzyme method for preparing laevo-rotation and dextro-rotation tryptophane 15N by resolving racemic tryptophase 15N

A technology of tryptophan and tryptophan, which is applied in the field of enzymatic separation of racemic tryptophan 15N to prepare left-handed and right-handed tryptophan 15N, which achieves the effects of gentle adsorption, fast flow rate and shortened operation cycle

Inactive Publication Date: 2007-08-29
SHANGHAI RES INST OF CHEM IND
View PDF6 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

No enzymatic resolution of racemic tryptophan 15 N makes L- and D-tryptophan 15 N's approach to reporting

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0046] Weigh 8.2 grams of N-acetyl-DL-tryptophan 15 N solid, dissolved with dilute NaOH, added water to make up to 333mL, then adjusted to pH=7 with dilute hydrochloric acid, added an equal volume of 10 -3 mol / L ZnCl 2 and an equal volume of pH=7.0 phosphate buffer to a total solution volume of 1000 mL. Then 0.3 g of aminoacylase enzyme powder was added to the solution. The mixed solution was reacted in a water-bath shaker at 37°C and 120 rpm for 48 hours. At this time, the hydrolysis rate was close to 100%, and N-acetyl-DL-tryptophan 15 N is split into L-tryptophan 15 N and N-acetyl-D-tryptophan 15 N. The reaction solution was concentrated under reduced pressure at 42°C to 1 / 3 of the original volume, extracted three times with an equal volume of ethyl acetate, and the L-tryptophan 15 N enters the aqueous phase, N-acetyl-D-tryptophan 15 N enters the organic phase to realize the product L-tryptophan 15 N and unreacted N-acetyl-D-tryptophan 15 N separation.

[0047] Pa...

Embodiment 2

[0050] Weigh 10 grams of N-acetyl-DL-tryptophan 15 N solid, dissolved with dilute NaOH, added water to make up to 333mL, then adjusted to pH=7 with dilute hydrochloric acid, added an equal volume of 10 -3 mol / L ZnCl 2 and an equal volume of pH=7.0 phosphate buffer to a total solution volume of 1000 mL. Then 0.4 g of aminoacylase enzyme powder was added to the solution. The mixed solution was reacted in a water-bath shaker at 37°C and 120 rpm for 60 hours. At this time, the hydrolysis rate was close to 100%, and N-acetyl-DL-tryptophan 15 N is split into L-tryptophan 15 N and N-acetyl-D-tryptophan 15 N. The reaction solution was concentrated under reduced pressure at 42°C to 1 / 5 of the original volume, extracted three times with an equal volume of ethyl acetate, and the L-tryptophan 15 N enters the aqueous phase, N-acetyl-D-tryptophan 15 N enters the organic phase to realize the product L-tryptophan 15 N and unreacted N-acetyl-D-tryptophan 15 N separation.

[0051] Pac...

Embodiment 3

[0054] Weigh 6 grams of N-acetyl-DL-tryptophan 15 N solid, dissolved with dilute NaOH, added water to make up to 333mL, then adjusted to pH=7 with dilute hydrochloric acid, added an equal volume of 10 -3 mol / L ZnCl 2 and an equal volume of pH=7.0 phosphate buffer to a total solution volume of 1000 mL. Then add 0.2 g of aminoacylase enzyme powder to the solution. The mixed solution was reacted in a water-bath shaker at 37°C and 120 rpm for 40 hours. At this time, the hydrolysis rate was close to 100%, and N-acetyl-DL-tryptophan 15 N is split into L-tryptophan 15 N and N-acetyl-D-tryptophan 15 N. The reaction solution was concentrated under reduced pressure at 42°C to 1 / 6 of the original volume, extracted three times with an equal volume of ethyl acetate, and L-tryptophan 15 N enters the aqueous phase, N-acetyl-D-tryptophan 15 N enters the organic phase to realize the product L-tryptophan 15 N and unreacted N-acetyl-D-tryptophan 15 N separation.

[0055] Pack 300mL mac...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

The present invention provides enzymatic resolution process of racemic tryptophase 15N to prepare levo-tryptophane 15N and dextro-tryptophane 15N. The process includes: compounding enzyme reaction liquid, enzyme hydrolysis to resolve N-acetyl-DL-tryptophane 15N, extraction to separate L-tryptophane 15N from N-acetyl-D-tryptophane 15N, resin separation of L-tryptophane 15N, refine L-tryptophane 15N product, hydrochloric acid hydrolysis to prepare D-tryptophane 15N product, resin separation of residual D-tryptophane 15N, refining D-tryptophane 15N product, and other steps. The present invention has simple process, high product yield, capacity of obtaining both chemical pure and optical pure L-tryptophane 15N and D-tryptophane 15N products, and other advantages.

Description

technical field [0001] The invention relates to a preparation method of biochemical products, in particular to an enzymatic method for splitting racemic tryptophan 15 N makes L- and D-tryptophan 15 N's method. Background technique [0002] L-Tryptophan is an important essential amino acid in humans and animals, and has a wide range of uses in medicine, food and feed additives. D-tryptophan is an unnatural amino acid with unique biological characteristics and plays an important role in the synthesis of short peptides. Replacing some L-amino acids in short peptides with D-tryptophan can produce special biological characteristics. When some amino acid antibiotics are mixed with D-tryptophan, they are difficult to be degraded by bacterial enzymes and will not produce drug resistance. , D-tryptophan and its derivatives are also used in the synthesis of new pollution-free amino acid pesticides, and the application prospects are very broad. At present, the research work on L an...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Patents(China)
IPC IPC(8): C12P13/22C12P41/00
Inventor 罗凤山吕志贤孙建春李良君杜晓宁宋明鸣
Owner SHANGHAI RES INST OF CHEM IND
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products