Synthetic resins or natural rubbers -- part of the class 520 ser – Synthetic resins – From carboxylic acid or derivative thereof
Reexamination Certificate
2000-06-13
2004-01-13
Hampton-Hightower, P. (Department: 1711)
Synthetic resins or natural rubbers -- part of the class 520 ser
Synthetic resins
From carboxylic acid or derivative thereof
C528S328000, C528S170000, C528S272000, C528S274000, C528S322000, C528S341000, C528S342000, C525S007000, C525S007100, C525S008000, C525S054100, C525S430000, C525S435000, C524S606000, C524S607000, C524S608000, C524S800000, C524S845000, C162S100000, C162S111000, C162S157100, C162S157300, C162S157600, C162S164300, C162S168200, C162S184000, C162S185000
Reexamination Certificate
active
06677427
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
This invention relates to polyamides, and processes for making and using the same. In particular, the polyamide is an enzymatic reaction product of a polyamine and diester. The present invention is further directed to cellulose products as well as creping adhesives and wet strength resins comprising the enzymatic reaction product, and processes for preparing the same.
2. Background of the Invention and Related Information
Polyamides are extensively used in the papermaking industry as wet strength agents or creping aids in the production of tissue and towel paper products. The polyamides are usually synthesized via chemical processes using chemical catalysts at high temperatures and in the presence of organic solvents. Chemical processes provide an economical means for high production of polymers. However, the chemical catalysts lack the high selectivity required for the production of polymers having suitable properties such as high purity and appropriate molecular weight. Also, chemical production of polymers contributes to pollution throughout and after synthesis [Chaudhary et al., Biotechnol. Prog., 13, 318-325, (1997)].
Enzymes possess high selectivity and fast catalytic rates under mild conditions [Dordick, Ann. N.Y. Acad. Sci., 672, 352-362, (1992)]. The high selectivity reduces side reactions and allows easier separation and/or purification of the desired product. In addition, the ability to catalyze various types of organic reactions under mild conditions (e.g., ambient temperatures and pressure) makes the commercial use of enzymes highly feasible and attractive [Chaudhary et al., Biotechnol. Prog., 13, 318-325, (1997)]. Furthermore, the discovery that enzymes can function in reverse to catalyze esterifications and transesterifications, rather than the customary degradation or hydrolysis, has made enzymatic synthesis a competitive alternative to chemical synthesis of polymers [Dordick, Ann. N.Y. Acad. Sci., 672, 352-362, (1992); Brazwell et al., J. Polym. Sci. Part A: Polym. Chem., 33, 89-95, (1995)].
The enzymatic synthesis of small molecules has been extensively demonstrated using lipase [Djeghaba et al., Tetrahedron Lett., 32, 761-762, (1991); Kanerva et al., Tetrahedron Assymm., 7, 1705-1716, (1996); Vorde et al., Tetrahedron Assym., 7, 1507-1513, (1996)]. Larger molecules, such as polyesters have also been synthesized enzymatically, using lipase as the catalyst and in the absence or presence of organic solvents.
Chaudary et al. [Biotechnol. Prog., 13, 318-325, (1997)] disclose bulk polymerization of polyesters under ambient conditions with low concentrations of biocatalyst.
Brazwell et al. [J. Polym. Sci. Part A: Polym. Chem., 33, 89-95, (1995)] describe enzyme-catalyzed polycondensation with pig pancreas lipase to produce aliphatic polyesters.
Linko et al. [Enzyme Microb. Technol., 17, 506-511, (1995)] describe the enzymatic polymerization of bis(2,2,2-trifluoroethyl) sebacate and aliphatic diols in a transesterification reaction to produce linear polyesters.
Binns et al. [J. Chem. Soc. Perkin Trans., 1, 899-904, (1993)] describe the enzymatic synthesis of a low-dispersity polyester from the polyesterification of adipic acid and butane-1,4-diol by a commercial lipase.
Geresh et al. [Biotechnol. Bioeng., 37, 883-888, (1991)] describe the synthesis of unsaturated polyesters using lipases from different sources and in two different organic solvents, acetonitrile and tetrahydrofuran.
Additionally, WO 94/12652 discloses the enzymatic synthesis of polyesters or polyester(amide)s in the absence of solvent and presence of lipase.
Despite the numerous chemical methods for producing polyamides, there still remains a need in the art for preparing polyamides that will provide relatively pure, high molecular weight polyamides in high yields.
SUMMARY OF THE INVENTION
The present invention relates to polyamides, and processes for preparing and using the same. The polyamide of the present invention is the enzymatic reaction product of a polyamine and diester. The present invention has found that enzymatic synthesis of polyamides provides high yields of relatively pure polyamides with high molecular weight.
In particular, the present invention is advantageous in providing a highly selective enzymatic process for the synthesis of polyamides with high molecular weight under mild conditions and without the need for extraneous solvents. In addition, the enzyme may be optionally recycled for further use.
The present invention provides a process for preparing a polyamide which comprises reacting at least one diester and at least one polyamine in the presence of hydrolytic enzyme wherein the hydrolytic enzyme is at least about 0.01% by weight based on the total weight of the diester and polyamine, and
the diester has the following general formula:
R
1
OOC—R—COOR
2
or
R
1
OOC—COOR
2
,
wherein R is a C
1
to C
20
hydrocarbyl group selected from one of alkyl, haloalkyl, alkylene, aryl, aralkyl, aralkylene, alkarylene, arylene, alkenyl or mixtures thereof; R
1
and R
2
are C
1
to C
22
hydrocarbyl group selected from alkyl, haloalkyl, alkylene, aryl, aralkyl, aralkylene, alkarylene, arylene, alkenyl or mixtures thereof; and wherein R
1
and R
2
may be the same or different; and
the polyamine has the following general formula:
H
2
N—R
3
—[X—R
4
]
n
—NH
2
,
wherein R
3
and R
4
are C
1
to C
6
hydrocarbyl group selected from one of alkyl, haloalkyl, alkylene, aryl, aralkyl, aralkylene, alkarylene, arylene, alkenyl or mixtures thereof; X is selected from one or none of heteroatom or non-heteroatom, wherein the non-heteroatom comprises amine, thiol, carbonyl, carboxyl or C
1
to C
6
hydrocarbyl group selected from one of alkanol, alkyl, haloalkyl, alkylene, aryl, aralkyl, aralkylene, alkarylene, arylene or alkenyl; n is from 0 to 40; and wherein R
3
and R
4
may be the same or different.
In one embodiment of the invention, R is a C
1
to C
4
alkyl group, R
1
is a C
1
to C
2
alkyl group, R
2
is a C
1
to C
2
alkyl group, R
3
is a C
2
to C
6
alkyl group, R
4
is a C
2
to C
6
alkyl group, X is CH
2
, O, S or NH, and n is 1 to 5.
In another embodiment of the invention, R is a C
2
to C
4
alkyl group, R
1
is a C
1
to C
2
alkyl group, R
2
is a C
1
to C
2
alkyl group, R
3
is a C
2
alkyl group, R
4
is a C
2
alkyl group, X is NH, and n is 1.
Additionally, the molecular weight of diesters of the present invention preferably range from about 100 to 1200 Daltons and most preferably from about 100 to 300 Daltons.
Suitable diesters of the present invention include dialkyl malonate, dialkyl fumarate, dialkyl maleate, dialkyl adipate, dialkyl glutarate, dialkyl succinate, dialkyl oxalate, dialkyl phenylmalonate or mixtures thereof.
The molecular weight of the polyamines of the present invention is preferably a range from about 40 to 10,000 Daltons and most preferably from about 40 to 2500 Daltons.
Suitable polyamines of the present invention include ethylenediamine (EDA), triethylene glycol diamine, bishexamethylenediamine (BHMT), hexamethylenediamine (HMDA), diethylenetriamine (DETA), triethylenetetramine (TETA), tetraethylenepentamine (TEPA), dipropylenetriamine (DPTA), tripropylenetetramine (TPTA), tetrapropylenepentamine (TPPA), N-methyl-bis-(aminopropyl)amine (MBAPA), spermine, spermidine, 1-phenyl-2,4-pentane diamine, 2-phenyl-1,3-propanediamine, phenylene diamine or mixtures thereof.
Enzymes of the present invention are obtained from natural (such as animals, plants, bacteria, yeast, fungi or virus) or synthetic sources (such as peptide synthesizer or expression vector). Natural sources include Candida species (such as
Candida antarctica
), Pseudomonas species (such as
Pseudomonas fluorescens
or Mucor species (such as
Mucor miehei
).
Suitable hydrolytic enzymes of the present invention are free or immobilized and include lipase, esterase or protease.
The hydrolytic enzyme is present in an amount preferably fr
Cheng Huai N.
Gu Qu-Ming
Maslanka William W.
Hampton-Hightower P.
Hercules Incorporated
Rossi Joanna
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