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WO1999024599A1 - N-acylation sous catalyse enzymatique d'aminoacides, d'hydrolysats proteiques et/ou de leurs derives - Google Patents

N-acylation sous catalyse enzymatique d'aminoacides, d'hydrolysats proteiques et/ou de leurs derives Download PDF

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Publication number
WO1999024599A1
WO1999024599A1 PCT/EP1998/006895 EP9806895W WO9924599A1 WO 1999024599 A1 WO1999024599 A1 WO 1999024599A1 EP 9806895 W EP9806895 W EP 9806895W WO 9924599 A1 WO9924599 A1 WO 9924599A1
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WO
WIPO (PCT)
Prior art keywords
fatty acid
acylation
derivatives
amino acids
acid derivatives
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/EP1998/006895
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German (de)
English (en)
Inventor
Anja Vonderhagen
Hans-Christian Raths
Eberhard Eilers
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Henkel AG and Co KGaA
BASF Personal Care and Nutrition GmbH
Original Assignee
Henkel AG and Co KGaA
Cognis Deutschland GmbH and Co KG
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Filing date
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Application filed by Henkel AG and Co KGaA, Cognis Deutschland GmbH and Co KG filed Critical Henkel AG and Co KGaA
Publication of WO1999024599A1 publication Critical patent/WO1999024599A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P13/00—Preparation of nitrogen-containing organic compounds
    • C12P13/02—Amides, e.g. chloramphenicol or polyamides; Imides or polyimides; Urethanes, i.e. compounds comprising N-C=O structural element or polyurethanes
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/32—Protein hydrolysates; Fatty acid condensates thereof
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins

Definitions

  • the present invention relates to an enzymatically catalyzed process for the N-acylation of amino acids, protein hydrolyzates and / or their derivatives by means of fatty acid derivatives in the presence of lipases and / or proteases, and the use of the compounds obtained as surfactants, in detergents and cleaning agents and in Environmental technology.
  • N-acylation products of amino acids, protein hydrolyzates and / or their derivatives are products known per se that have been acylated on the nitrogen atom.
  • Their technical synthesis is currently carried out practically exclusively via N-acylation using fatty acid chlorides in an alkaline medium after the Schotten-Baumann reaction.
  • a disadvantage of this process is that, on the one hand, the fatty acid chlorides are very expensive starting materials which, on the other hand, cause the N-acylation products to be contaminated with traces of AOX, which makes their use as particularly mild surfactants in the cosmetic field more difficult.
  • the object of the present invention was. to provide an enzymatically catalyzed process for the N-acylation of amino acids, protein hydrolyzates and / or their derivatives, which provides the N-acylated products in good yields and in shorter reaction times.
  • it should be a simple, one-step process that can also be carried out using starting materials available on the market.
  • the present invention relates to a process for the enzymatic N-acylation of amino acids, protein hydrolyzates and / or their derivatives, characterized in that for the N-acylation fatty acid derivatives selected from that of fatty acid esters of mono- and / or difunctional alcohols, fatty acid salts and fatty acid anhydrides formed group and used as enzymes lipases and / or proteases.
  • the fatty acid derivatives to be used according to the invention are preferably derived from fatty acids having 6 to 22 carbon atoms. These fatty acids are to be understood as meaning aliphatic carboxylic acids of the formula (I)
  • Typical examples are caproic acid, caprylic acid, 2-ethylhexanoic acid, capric acid, lauric acid, isotridecanoic acid.
  • Fatty acids with 12 to 18 carbon atoms and in particular technical fatty acids with 12 to 18 carbon atoms such as, for example, coconut, palm, palm kernel or tallow fatty acids are preferred.
  • fatty acid esters of onofunctional alcohols such aliphatic alcohols having 1 to 22 carbon atoms, preferably having 1 to 4 carbon atoms, are suitable as monofunctional alcohols.
  • Methanol is particularly preferred as the monofunctional alcohol, i.e. the methyl esters of the corresponding fatty acids are particularly preferred.
  • methyl esters are existing industrial products.
  • Suitable monofunctional alcohols are also diglycerides.
  • ethylene glycol, propylene glycol, polyethylene glycol, polypropylene glycol and monoglycerides are suitable as difunctional alcohols.
  • Particularly suitable salts of the fatty acids are the alkali and / or alkaline earth metal salts of the fatty acids, such as sodium laurate.
  • the group of fatty acid anhydrides is a well-known class of compounds which can be prepared in a conventional manner by the intermolecular elimination of water from two fatty acids of the type described.
  • the fatty acid derivatives can also be used in a mixture with free fatty acids, the mixtures at least 20% by weight, preferably at least 40% by weight. and in particular at least 50% by weight, which contain fatty acid derivatives and the rest free fatty acids.
  • Amino acids, protein hydrolyzates and / or their derivatives are subjected to acylation.
  • the amino acids can be of natural and / or technical origin. It can be alpha and / or beta amino acids.
  • amino acids examples include alpha- and beta- alanine, arginine, asparagine, aspartic acid, cysteine, cystine, 3,5-dibromtyrosine, 3,5-diiodotyrosine, glutamic acid, glutamine, glycine, N-methylglycine (sarcosine), histidine, hydroxylysine , Hydroxyproline, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Proline, Serine, Threonine, Thyroxine, Tryptophan, Tyrosine and Valine.
  • Protein hydrolysates are degradation products of animal or vegetable proteins, for example collagen, elastin or keratin and preferably almond and potato protein and in particular wheat, rice and soy protein, which are cleaved by acidic, alkaline and / or enzymatic hydrolysis.
  • the protein hydrolyzates preferably have an average molecular weight in the range from 130 to 4000, preferably 400 to 3000.
  • Vegetable protein hydrolyzates based on wheat gluten or rice protein are preferably used, the production of which is described in the two German patents DE-Cl 19502167 and DE-Cl 19502168 (Henkel).
  • the salts and / or esters are preferably used as derivatives of amino acids or protein hydrolyzates, in particular the alkali and / or alkaline earth salts and also the esters of monofunctional alcohols having 1 to 4 carbon atoms, such as methanol. If the underlying amino acids have two carboxyl groups, such as glutamic acid, the mono- and / or the disalts or the mono- and / or the diesters can be used. If the amino acid esters have been stabilized with hydrochloride, the presence of an amine such as triethylamine is recommended when using them, so that the nitrogen of the underlying amino acid is easily accessible for acylation.
  • glutamic acid, aspartic acid, glycine, N-methylglycine and / or phenylalanine and the derivatives of the amino acids to the mono- and / or disodium salt of glutamic acid, the mono- and / or disodium salt of aspartic acid, the Mono- and / or dimethyl ester of glutamic acid and the methyl ester of phenylalanine are used.
  • the molar ratio of fatty acid derivatives to amino acids, protein hydrolyzates and / or their derivatives is preferably in the range from 1:10 to 10: 1, in particular from 2: 1 to 1: 2, calculated as per mole of available acyl group and based on per mole of nitrogen group to be acylated in the amino acid, protein hydrolyzate and / or their derivative.
  • N-acylation is catalyzed by the presence of enzymes.
  • the enzymes are lipases and / or proteases, preferably lipases. Examples of suitable lipases can be found in the already cited international application WO 90/14429, which are hereby included in the disclosure content. Lipases from Cand. cylindracea, cand. lipolytica, cand. rugosa, cand. antartica, cand.
  • chromobacterium viscosum chromobacterium viscosum, geotrichum viscosum, geotrichum candidum, mucor javanicus, mucor miehei, porcine pancreas, pseudomonas spieces., pseudomonas fluorescens, pseudomonus rhopushia, pseudomonas cepopia delemar, rhizopus niveus, rhizopus oryzae, aspergillus niger, penicillium roqueforti, penicillium cambertii.
  • the lipases SP 523 R , SP 524 R , SP 525 R , SP 526R, Novozym 435 an immobilized lipase from candi.
  • Lipozym IM R an immobilized lipase from mucor miehei
  • all commercial products from are particularly advantageous Novo Nordisk, as well as Chirazyme Ll to L8 R , commercial products from Boehringer Mannheim.
  • proteases are alpha-chymotrypsin (bovine pancreas), proteinase (bacillus subtilis), subtilisin Calsberg (bacillus subtilis var. Biotecus A).
  • the lipases and / or proteases can be native or immobilized on a carrier.
  • the lipases and / or proteases are preferably used as catalysts in amounts of 0.001 to 50% by weight, in particular in amounts of 1 to 30% by weight - calculated as lipase and / or protease in native or immobilized form and based on the total amount of starting materials to be converted - present. If the lipases and / or proteases are added in native form, amounts of 0.001 to 15% by weight, based on the total amount of starting materials to be converted, are recommended.
  • the enzymatically catalyzed N-acylation is preferably carried out in the presence of one or more organic solvents.
  • Suitable organic solvents are those which themselves are not converted as substrates by the enzymes used.
  • the solvents can both form a uniform phase and a two-phase system, since the lipases and / or proteases are also able to catalyze reactions at the interface.
  • Suitable solvents are secondary and tertiary alcohols, ketones such as acetone, ethyl methyl ethyl ketone and butyl methyl ketone, ethereal solvents such as dialkyl ether and tetrahydrofuran, pure hydrocarbons such as pentane, hexane, dimethylformamide, dimethyl sulfoxide and mixtures with one another.
  • the organic solvents can contain up to 30% by weight of water as solvent.
  • the enzymatically catalyzed N-acylation is preferably carried out at temperatures in the range from 20 to 100 ° C., in particular at 50 to 70 ° C.
  • the process can be carried out in different versions.
  • the amino acids or their derivatives are predissolved in the solvent or in the solvent mixture.
  • the fatty acid derivatives and the lipases and / or proteases are then added.
  • the reaction mixture is brought to the desired reaction temperature under reflux of the solvent.
  • the reaction mixture is filtered, whereby lipases and / or proteases and possibly other insoluble constituents are retained.
  • the desired product is obtained from the filtrate by removing the solvent by distillation.
  • the fatty acid derivatives are suspended in the solvent and heated.
  • the amino acid or its derivatives and the lipase and / or protease are added with stirring.
  • the further procedure corresponds to the first variant.
  • the fatty acid derivatives and the amino acids or their derivatives are introduced together in the solvent mixture and then the lipase and / or protease are added as catalysts.
  • the pH of the solution must be observed.
  • the pH should be chosen so that the free nitrogen atom of the amino acid, protein hydrolyzates or their derivatives is not yet protonated.
  • the person skilled in the art can obtain an indication of the pH values to be selected from the corresponding pKs values of the amino acids, protein hydrolyzates or their derivatives.
  • the present invention further relates to the use of the compounds prepared according to the invention as a skin-friendly surfactant, in particular in detergents and cleaning agents, for example in the textile industry, in the food industry, for the production of detergents or for the production of cosmetic preparations. Since it is a skin-friendly surfactant, it is particularly suitable for cosmetic preparations.
  • Cosmetic preparations are understood to be hair and body care compositions which contain the surfactants obtainable according to the invention in amounts of 1 to 35% by weight.
  • the cosmetic preparations can of course contain other surfactants as well as usual components in usual amounts.
  • Another object of the present invention relates to the use of the compounds prepared according to the invention as a surfactant in environmental technology, in particular for soil remediation and water treatment.
  • the crude product was identified by NMR spectroscopy and by means of GC analysis.
  • the yield of the crude product was 52% by weight after 24 hours and 65% by weight after 36 hours, based on the solids.
  • High-purity product can be obtained by column chromatography or by recrystallization.

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
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  • Chemical Kinetics & Catalysis (AREA)
  • Microbiology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Biotechnology (AREA)
  • Biochemistry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Molecular Biology (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

La présente invention concerne un procédé sous catalyse enzymatique pour la N-acylation d'aminoacides, d'hydrolysats protéiques et/ou de leurs dérivés au moyen de dérivés d'acides gras en présence de lipases et/ou de protéases, ainsi que l'utilisation des composés obtenus comme tensioactifs, dans des détergents et dans le génie de l'environnement.
PCT/EP1998/006895 1997-11-10 1998-10-30 N-acylation sous catalyse enzymatique d'aminoacides, d'hydrolysats proteiques et/ou de leurs derives Ceased WO1999024599A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE19749555.9 1997-11-10
DE1997149555 DE19749555A1 (de) 1997-11-10 1997-11-10 Enzymatisch-katalysierte N-Acylierung von Aminosäuren, Proteinhydrolysaten und/oder deren Derivaten

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WO1999024599A1 true WO1999024599A1 (fr) 1999-05-20

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WO (1) WO1999024599A1 (fr)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2024246100A1 (fr) 2023-05-31 2024-12-05 Basf Se Aminoacylase et ses procédés d'utilisation

Citations (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2252281A1 (de) * 1971-10-28 1973-05-03 Kyowa Hakko Kogyo Kk Enzymatisch hydrolisierte zusammensetzung und deren derivate aus hautlappen
FR2254554A1 (fr) * 1973-12-12 1975-07-11 Ajinomoto Kk
WO1990014429A1 (fr) * 1989-05-25 1990-11-29 Novo Nordisk A/S Procede pour la preparation d'amino-acides n-acyle et des amides d'amino-acides n-acyle
WO1991019002A1 (fr) * 1990-06-01 1991-12-12 Carlbiotech Ltd. A/S Procede d'enrichissement chiral d'amines primaires asymetriques
JPH05153985A (ja) * 1991-11-29 1993-06-22 Lion Corp 脂肪酸アミドの製造方法
WO1994026919A1 (fr) * 1993-05-06 1994-11-24 Gist-Brocades N.V. Synthese enzymatique de ceramides et de ceramides hybrides
DE19546533A1 (de) * 1995-12-13 1997-06-19 Degussa Verfahren zur Herstellung von N-Acetyl-D,L-alpha-aminocarbonsäuren
DE19603575A1 (de) * 1996-02-01 1997-08-07 Bayer Ag Verfahren zur Herstellung von optisch aktiven Aminen

Patent Citations (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2252281A1 (de) * 1971-10-28 1973-05-03 Kyowa Hakko Kogyo Kk Enzymatisch hydrolisierte zusammensetzung und deren derivate aus hautlappen
FR2254554A1 (fr) * 1973-12-12 1975-07-11 Ajinomoto Kk
WO1990014429A1 (fr) * 1989-05-25 1990-11-29 Novo Nordisk A/S Procede pour la preparation d'amino-acides n-acyle et des amides d'amino-acides n-acyle
WO1991019002A1 (fr) * 1990-06-01 1991-12-12 Carlbiotech Ltd. A/S Procede d'enrichissement chiral d'amines primaires asymetriques
JPH05153985A (ja) * 1991-11-29 1993-06-22 Lion Corp 脂肪酸アミドの製造方法
WO1994026919A1 (fr) * 1993-05-06 1994-11-24 Gist-Brocades N.V. Synthese enzymatique de ceramides et de ceramides hybrides
DE19546533A1 (de) * 1995-12-13 1997-06-19 Degussa Verfahren zur Herstellung von N-Acetyl-D,L-alpha-aminocarbonsäuren
DE19603575A1 (de) * 1996-02-01 1997-08-07 Bayer Ag Verfahren zur Herstellung von optisch aktiven Aminen

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
CHEMICAL ABSTRACTS, vol. 122, no. 24, 12 June 1995, Columbus, Ohio, US; abstract no. 293910, JAUREGI, PAULA ET AL: "Enzymic approach to the synthesis of amino acid based surfactants" XP002096338 *
CONF. APPL. BIOCATAL., THREE-DAY SYMP. (1994), 65-7 PUBLISHER: INST. CHEM ENG., RUGBY, UK. CODEN: 60NWA5 *
DATABASE WPI Section Ch Week 9329, Derwent World Patents Index; Class D16, AN 93-231502, XP002096339 *

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2024246100A1 (fr) 2023-05-31 2024-12-05 Basf Se Aminoacylase et ses procédés d'utilisation

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Publication number Publication date
DE19749555A1 (de) 1999-05-12

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