WO2009066975A1 - A method for producing adipate ester - Google Patents
A method for producing adipate ester Download PDFInfo
- Publication number
- WO2009066975A1 WO2009066975A1 PCT/MY2008/000093 MY2008000093W WO2009066975A1 WO 2009066975 A1 WO2009066975 A1 WO 2009066975A1 MY 2008000093 W MY2008000093 W MY 2008000093W WO 2009066975 A1 WO2009066975 A1 WO 2009066975A1
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- WO
- WIPO (PCT)
- Prior art keywords
- mixture
- adipate ester
- adipate
- adipic acid
- alcohol
- Prior art date
Links
- -1 adipate ester Chemical class 0.000 title claims abstract description 26
- 238000004519 manufacturing process Methods 0.000 title description 8
- WNLRTRBMVRJNCN-UHFFFAOYSA-N adipic acid Chemical compound OC(=O)CCCCC(O)=O WNLRTRBMVRJNCN-UHFFFAOYSA-N 0.000 claims abstract description 51
- 238000000034 method Methods 0.000 claims abstract description 26
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims abstract description 21
- 239000001361 adipic acid Substances 0.000 claims abstract description 21
- 235000011037 adipic acid Nutrition 0.000 claims abstract description 21
- 239000000203 mixture Substances 0.000 claims abstract description 20
- 102000004190 Enzymes Human genes 0.000 claims abstract description 17
- 108090000790 Enzymes Proteins 0.000 claims abstract description 17
- 238000010993 response surface methodology Methods 0.000 claims abstract description 11
- 238000005457 optimization Methods 0.000 claims abstract description 9
- 241000222120 Candida <Saccharomycetales> Species 0.000 claims abstract description 4
- 108010048733 Lipozyme Proteins 0.000 claims abstract description 4
- 108010084311 Novozyme 435 Proteins 0.000 claims abstract description 4
- 241000235403 Rhizomucor miehei Species 0.000 claims abstract description 4
- FCCDDURTIIUXBY-UHFFFAOYSA-N lipoamide Chemical compound NC(=O)CCCCC1CCSS1 FCCDDURTIIUXBY-UHFFFAOYSA-N 0.000 claims abstract description 4
- 241000222175 Diutina rugosa Species 0.000 claims abstract description 3
- 238000002156 mixing Methods 0.000 claims abstract description 3
- 108090001060 Lipase Proteins 0.000 claims description 19
- 102000004882 Lipase Human genes 0.000 claims description 19
- 239000004367 Lipase Substances 0.000 claims description 18
- 235000019421 lipase Nutrition 0.000 claims description 18
- 239000011942 biocatalyst Substances 0.000 abstract description 8
- 108010093096 Immobilized Enzymes Proteins 0.000 abstract description 6
- 239000000047 product Substances 0.000 description 17
- 238000006243 chemical reaction Methods 0.000 description 14
- 150000002148 esters Chemical class 0.000 description 13
- 150000001875 compounds Chemical class 0.000 description 8
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 238000003786 synthesis reaction Methods 0.000 description 6
- 239000003054 catalyst Substances 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 239000011541 reaction mixture Substances 0.000 description 5
- 238000000926 separation method Methods 0.000 description 5
- 238000005886 esterification reaction Methods 0.000 description 4
- 239000003960 organic solvent Substances 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 230000015556 catabolic process Effects 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- 230000036541 health Effects 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 231100000053 low toxicity Toxicity 0.000 description 3
- 239000000314 lubricant Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 238000004448 titration Methods 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- XDTMQSROBMDMFD-UHFFFAOYSA-N Cyclohexane Chemical compound C1CCCCC1 XDTMQSROBMDMFD-UHFFFAOYSA-N 0.000 description 2
- OFOBLEOULBTSOW-UHFFFAOYSA-N Malonic acid Chemical compound OC(=O)CC(O)=O OFOBLEOULBTSOW-UHFFFAOYSA-N 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 238000013528 artificial neural network Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- ZXEKIIBDNHEJCQ-UHFFFAOYSA-N isobutanol Chemical compound CC(C)CO ZXEKIIBDNHEJCQ-UHFFFAOYSA-N 0.000 description 2
- VLKZOEOYAKHREP-UHFFFAOYSA-N n-Hexane Chemical compound CCCCCC VLKZOEOYAKHREP-UHFFFAOYSA-N 0.000 description 2
- 238000007086 side reaction Methods 0.000 description 2
- 238000012549 training Methods 0.000 description 2
- 238000005033 Fourier transform infrared spectroscopy Methods 0.000 description 1
- 239000004164 Wax ester Substances 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- WNLRTRBMVRJNCN-UHFFFAOYSA-L adipate(2-) Chemical compound [O-]C(=O)CCCCC([O-])=O WNLRTRBMVRJNCN-UHFFFAOYSA-L 0.000 description 1
- 150000001335 aliphatic alkanes Chemical class 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 238000000540 analysis of variance Methods 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000008199 coating composition Substances 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 230000007797 corrosion Effects 0.000 description 1
- 238000005260 corrosion Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000005265 energy consumption Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 125000004185 ester group Chemical group 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000002329 infrared spectrum Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 235000019386 wax ester Nutrition 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
Classifications
-
- 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
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/62—Carboxylic acid esters
-
- 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
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/64—Fats; Fatty oils; Ester-type waxes; Higher fatty acids, i.e. having at least seven carbon atoms in an unbroken chain bound to a carboxyl group; Oxidised oils or fats
- C12P7/6436—Fatty acid esters
-
- 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
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/64—Fats; Fatty oils; Ester-type waxes; Higher fatty acids, i.e. having at least seven carbon atoms in an unbroken chain bound to a carboxyl group; Oxidised oils or fats
- C12P7/6436—Fatty acid esters
- C12P7/6445—Glycerides
- C12P7/6454—Glycerides by esterification
Abstract
The present invention provides a method of producing a purified wax adipate ester comprising the steps of: (a) mixing adipic acid with an alcohol, (b) adding a highly stable biocatalyst such as an immobilized enzyme to form a homologous mixture, (c) incubating the mixture and (d) obtaining a purified adipate ester. The method further comprises optimization using Response Surface Methodology (RSM). Preferred enzymes include Candida rugosa, Rhizomucor miehei (Lipozyme RM IM), and Candida antartica (Novozym 435).
Description
A METHOD FOR PRODUCING ADIPATE ESTER
FIELD OF INVENTION
The present invention relates to the development of a highly stable biocatalyst such as immobilized enzyme for the synthesis of high added-value esters. More particularly, the present invention provides a process for producing wax ester, preferbally adipate esters.
BACKGROUND OF THE INVENTION
Adipate esters which are derived from compounds of C6 straight-chain dicarboxylic adipic acid and alcohol are of considerable industrial interest compared with the ordinary esters especially in petrochemical industries. The excellent properties of adipic esters such as its low toxicity, good thermal stability, low volatility and high biodegradability make it a very useful compound and significant to many industrial applications especially in domestic, health care products, and lubricant industries.
Adipate esters are produced by reacting an adipic acid and an alcohol at high temperatures in the presence of metal or chemical catalysts. This method leads to undesirable side reactions and degradation of esters. The use of those catalysts exposed to toxicity and corrosion. Reaction with homogenous chemical catalysts are usually time consuming and also give relatively low yields. Esterification reaction is a reversible process; hence the long time reaction may result in hydrolysis reaction.
At the present, the use of homogenous chemical catalysts for producing adipate esters may lead to several problems such as separation of products, hazards in handling of the corrosive acids, high energy consumption and degradation of esters. Thus, interests have grown on the use of green synthesis of esters in organic medium catalyzed by using immobilized enzyme.
However, for future industrial scale enzymatic production of adipate esters, it would be beneficial to simplify the reaction conditions as much as possible. Recently, optimization of enzyme-catalyzed production of various esters by Response Surface Methodology (which is an efficient statistical technique for optimization of multiple variables) and Artificial Neural Network (which estimates the response based on the trained data) has been investigated.
SUMMARY OF THE INVENTION
Accordingly, the object of the invention relates to a method of producing purified wax adipate ester. The method includes the steps of; mixing adipic acid with alcohol to obtain a mixture, adding a solution of enzyme into the mixture, shaking the mixture to form a homologous mixture, incubating the mixture for at least 2 hours, obtaining a product containing purified adipate ester; calculating percentage of the adipate ester;
Further to that, the mixture is incubated between 30 0C and 70 °C and the enzyme consists of immobilized lipases. The immobilized lipases that is preferred includes Candida rugosa, Rhizomucor miehei (Lipozyme RM IM), and Candida antartica (Novozym 435). Based on the method, the obtained product is adipate esters and the said product having at least a percentage between 35% and 90% of purified adipate ester(s). The method also further includes optimization using Response Surface Methodology (RSM), wherein the optimization produced a yield of at least 95% and above.
The Adipate esters which is produced from methods above having excellent properties of adipic esters such as its low toxicity, good thermal stability, low volatility and high biodegradability make it a very useful compound and significant to many industrial applications especially in domestic, health care products, and lubricant industries. The invention will be formulated as one of the ingredient in wood coating formulations.
Another application is as a plastic syringe which will be used in medical area because of its excellent properties. This invention was produced at mild conditions, which prevent degradation of starting materials and reduce side reactions. The use of immobilized enzyme has become a valid approach due to its special features which allow the reutilization of the enzyme and better separation of products. Furthermore, the percentage of yield is high and optimization was done using RSM which reduced number of experimental runs needed to provide sufficient information for statistically acceptable result.
BRIEF DESCRIPTION OF THE DRAWINGS
Figure 1 represents percentage conversion of adipic acid and alcohol in various temperatures.
Figure 2 represents the relative yield of the product obtained in various temperatures.
Figure 3 represents infrared spectrum of the adipate ester.
Figure 4 represents schematic diagram of artificial neural network (ANN)
Figure 5 represents mean squared error vs. epoch (cycle) during the training process
Figure 6 represents ANN correlation between the observed and predicted adipte ester yield.
Figure 7 represents response surface plot showing the effect of molar ratio, time and their interaction on the synthesis of adipate ester.
Figure 8 represents response surface plot showing the effect of temperature, reaction time and their interaction on the synthesis of adipate ester
BRIED DESCRIPTION OF THE INVENTION
The present invention discuss on the development of a highly stable biocatalyst such as immobilized enzyme for the synthesis of high added-value esters. The use of immobilized enzyme has become a valid approach due to its special features which allow the reutilization of the enzyme and better separation of products. Application of lipases in various biochemical modifications of fats and oils is well established, several dicarboxylic adipate esters produced in the present invention are useful as surfactants or chemicals additives. Accordingly, the object of the invention relates to a method for producing a high quality and purity wax adipate esters. In addition to that, the present invention also produces a high yield of adipate esters by esterification reaction of dicarboxylic acid preferably adipic acid with at least one alcohol in the presence of lipase. Further to this, the invention describes in detail on an improve method to carry out the above method on large-scale basis to produce a product such as adipate ester(s). The product is optimized by using RSM/ANN.Further to the method, the present invention related to a method for producing adipate ester by enzymatically esterifiying dicarboxylic acid preferably adipic acid with at least one alcohol which contains 2 to 18 carbons per molecule. In the preferred embodiment of the present invention, the adipic acid is derived from cyclohexane. In another embodiment of the present invention the adipic acid may be derived from other petrochemical-based compounds. The alcohol used in the present invention can be linear or branched alcohol contains 2 to 18 carbons per molecule.Adipate ester(s) is developed by mixing adipic acid and alcohol in a shaker. A sutaible mixture is obtain when adipic acid and alcohol is placed in a shaker and continuously shaking the shaker at temperature in the range from about 30 °C to 70 0C. Further to this, an esterification reaction is carried out with organic solvent as a medium and with enzyme as the biocatalyst. An immobilized lipase enzyme is chosen as a biocatalyst in the reaction mixture to facilitate the esterification reaction. The immobilized lipase is recycled with the selectivity of the immobilized lipase and purity of the product is controlled.
The effect of parameters on the reaction and their interaction on the production of ester is investigated by use of RSM, Central Composite Rotatable Design (CCRD). To train an ANN model a set of data containing inputs and outputs are fed. The same experimental data used in each RSM design is used as the training data of the ANN. The excellent properties of adipic esters such as its low toxicity, good thermal stability, low volatility and high biodegradability make it a very useful compound and significant to many industrial applications especially in domestic, health care products, and lubricant industries.
DETAILED DESCRIPTION OF THE INVENTION
The invention will now be described in more detail by reference to the following Figures and Examples. The following examples are provided for illustrative purposes only and are not intended to limit the invention.
According to the present invention, process for producing adipate ester comprises esterifying adipic acid compound with at least one alcohol in the presence of lipase as a catalyst and an organic solvent as the medium. In the preferred embodiment of the present invention, stated adipic acid is derived from petrochemical-based compounds whereas said alcohol is an alcohol with 2 to 18 carbon atoms per molecule.
Continuous shaking is applied to the reaction mixture and the mixture is allowed to proceed for 2 hours. Later, the reaction mixture is separated from the biocatalyst by filtration. The separated biocatalyst is then recycled and washed with organic solvent.
In the preferred embodiment of the present invention, the immobilized lipase is used. Immobilized lipase has the advantages by easy separation from the product and the reusability is allowed. Lipase is highly selective towards certain bonds and specific with respect to their substrates. Easy separation will permit efficient handling of the process while the reusability of lipase will allow for cost reduction and higher production.
The immobilize lipases that used in the present invention are Candida antartica (Novozym 435) or Rhizomucor miehei (Lipozyme RM IM). Both lipases are measured in the same amount if applied. The protein content of the mixture is controlled to maximize the adipate ester product.
In addition, it is preferred to use adipic acid compound derived from petrochemical- based cyclohexane.The ratio of adipic acid to alcohol is set to 1:2. In the preferred embodiment of the present invention, to get highest percentage conversion of adipic acid and alcohol to adipate ester, adipic acid and alcohol will be supplied at a mole ratio in the range of 1 : 1 to 1 :6 with preferably 1 :2 for short chain and 1 :4 for medium chain length of alcohol used. The reaction is carried out in temperature with range from 30 0C to 70 0C with preferably 50 0C. In the present invention, the mixture undergoes continuous shaking in controlled temperature. Changing in the reaction temperature can be assigned to its effect on substrate solubility as well as its direct influences on the reaction rate, enzyme stability and activity.The percentage conversion is calculated based on the titration result compared with relative volume of substrate to product. In the present invention, the titration is performed after filtration of biocatalyst. NaOH neutralized the acidity of the reaction product until in excess to pH 10.
Adipate ester obtainable from the method according to the present invention is dimethyl- 1 -propyl) adipate which presented by formula (1):
(CH3)2CHCH2O2C(CH2)4CO2CH2CH(CH3)2 Formula 1
The present invention can be performed in various ways, but certain detailed routes embodying the present invention will be illustrated in the following examples.
EXAMPLE 1
A batchwise operation was carried out on a laboratory scale. Adipic acid (2.0 mmol) was weighed and placed in 6 sample vials each. Isobutanol (4.0 mmol) was added into the each vials followed by n-hexane (15.0 ml) as solvent. Then, lipase (0.3g) was added into three of the six vials and all vials were closed tightly. The reaction mixture of samples and control (sample without lipases) were incubated at 30 0C in a horizontal water bath shaker with shaking speed of 150 rpm continuously for 2 hours.
The reaction was terminated after 2 hours by diluting the sample with 3.5 ml of ethanol/acetone (1:1 vol / vol). The remaining free adipic acid in the reaction mixture was determined using a titration with 0.1M of NaOH until an end point of pH 10.0 which was detected by auto-titrator Metier-Toledo Metrohm equipment. The activity of lipase of each reaction was expressed as percentage of converted adipic acid. After that, the percentage of yield and relative yield were calculated.
The product has a relative yield about 88.36%. FT-IR: showed the sharp peak at 1736.00 cm-1 represented the existence of (C=O) bond for ester. The highest intensity for this peak strongly proved the presence of ester group in the compound. The presence of (C-O) bond in the compound was shown by the peak at 1176.00 cm-1 while the peak for alkyl groups were shown at 1464.00 cm-1 and 1378.00 cm-1, and the peak for alkanes was shown at 2960.00 cm-1.
EXAMPLE 2
Example 1 was repeated. The mixture was heated to 300C in a water-bath shaker. The reaction was allowed to proceed for 1 h. The yield was about 39.16%.
EXAMPLE 3
Example 1 was repeated. The mixture without organic solvent was heated to 55 0C in a water-bath shaker. The reaction was allowed to proceed for 2 h. The yield is about 78.03%.
EXAMPLE 4
Fitting of the data to the various models (linear, two factorial, quadratic and cubic) and their subsequent analysis of variance (optimization study) showed that the synthesis of adipate ester was suitably described with quadratic polynomial model. The very small p- value (0.0001) and a suitable coefficient of determination, R2 = 0.9660, showed that the quadratic polynomial model was highly significant and sufficient to present the actual relationship between the response and the significant variables.
Claims
1. A method of producing purified wax adipate ester , wherein the method comprising the steps of: a) mixing adipic acid with alcohol to obtain a mixture, b) adding a solution of enzyme into the mixture from step (a) c) shaking the mixture from step (b) to form a homologous mixture; d) incubating the mixture from step (c) for at least 2 hours; e) obtaining a product containing purified adipate ester; f) calculating percentage of the adipate ester;
2. The method as claimed in claiml, wherein the mixture is incubated between 30 0C and 70 0C.
3. The method as claimed in claiml, wherein the enzyme consists of immobilized lipases.
4. The method as claimed in claim 3, wherein the immobilized lipases including Candida rugosa, Rhizomucor miehei (Lipozyme RM IM), and Candida antartica (Novozym 435).
6. The method as claimed in claiml, wherein the product obtained having at least a percentage between 35% and 90% of purified adipate ester.
7. The method as claimed in claiml further includes optimization using Response Surface Methodology (RSM), wherein the optimization produced a yield at least 95% and above.
8. Adipate esters is produced from any of the preceding method claims 1 to 7.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| MYPI20072080 | 2007-11-23 | ||
| MYPI20072080A MY144876A (en) | 2007-11-23 | 2007-11-23 | A method for producing adipate ester |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO2009066975A1 true WO2009066975A1 (en) | 2009-05-28 |
Family
ID=40667701
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/MY2008/000093 WO2009066975A1 (en) | 2007-11-23 | 2008-09-03 | A method for producing adipate ester |
Country Status (2)
| Country | Link |
|---|---|
| MY (1) | MY144876A (en) |
| WO (1) | WO2009066975A1 (en) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2015060862A1 (en) * | 2013-10-25 | 2015-04-30 | Empire Technology Development Llc | Methods of producing dicarbonyl compounds |
| US9982094B2 (en) | 2013-10-22 | 2018-05-29 | Empire Technology Development Llc | Compounds and methods for producing nylon 6 |
| US9988491B2 (en) | 2013-10-22 | 2018-06-05 | Empire Technology Development Llc | Methods and compounds for producing nylon 6,6 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SG123626A1 (en) * | 2004-12-17 | 2006-07-26 | Univ Putra Malaysia | Production of wax esters |
| EP1775344A2 (en) * | 2005-10-11 | 2007-04-18 | Beijing University of Chemical Technology | Lipase, its gene, the strain and the application of this lipase |
-
2007
- 2007-11-23 MY MYPI20072080A patent/MY144876A/en unknown
-
2008
- 2008-09-03 WO PCT/MY2008/000093 patent/WO2009066975A1/en active Application Filing
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SG123626A1 (en) * | 2004-12-17 | 2006-07-26 | Univ Putra Malaysia | Production of wax esters |
| EP1775344A2 (en) * | 2005-10-11 | 2007-04-18 | Beijing University of Chemical Technology | Lipase, its gene, the strain and the application of this lipase |
Non-Patent Citations (2)
| Title |
|---|
| BASRI, M. ET AL.: "Comparison of estimation capabilities of response surface methodology (RSM) with artificial neural network (ANN) in lipase-catalyzed synthesis of palm-based wax ester", BMC BIOTECHNOLOGY, vol. 7, no. 53, 2007, pages 14, Retrieved from the Internet <URL:http://www.6iomedcentraLcomlI472-6750J7/53> * |
| RAHMAN, M. B. A. ET AL.: "Enzymatic synthesis of methyl adipate ester using lipase from Candida rugosa immobilised on Mg, Zn and Ni of layered double hydroxides (LDHs)", JOURNAL OF MOLECULAR CATALYSIS B: ENZYMATIC, vol. 50, 2008, pages 33 - 39 * |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9982094B2 (en) | 2013-10-22 | 2018-05-29 | Empire Technology Development Llc | Compounds and methods for producing nylon 6 |
| US9988491B2 (en) | 2013-10-22 | 2018-06-05 | Empire Technology Development Llc | Methods and compounds for producing nylon 6,6 |
| WO2015060862A1 (en) * | 2013-10-25 | 2015-04-30 | Empire Technology Development Llc | Methods of producing dicarbonyl compounds |
| US10131610B2 (en) | 2013-10-25 | 2018-11-20 | Empire Technology Development Llc | Methods of producing dicarbonyl compounds |
Also Published As
| Publication number | Publication date |
|---|---|
| MY144876A (en) | 2011-11-30 |
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