US3622515A - Electrophotographic liquid developer having a proteolytic enzyme - Google Patents

Electrophotographic liquid developer having a proteolytic enzyme Download PDF

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Publication number
US3622515A
US3622515A US819324A US3622515DA US3622515A US 3622515 A US3622515 A US 3622515A US 819324 A US819324 A US 819324A US 3622515D A US3622515D A US 3622515DA US 3622515 A US3622515 A US 3622515A
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United States
Prior art keywords
proteolytic enzyme
liquid developer
toner
finely divided
electrophotographic
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Expired - Lifetime
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US819324A
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English (en)
Inventor
Yasuo Tamai
Seiichi Taguchi
Satoru Honjo
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Fujifilm Holdings Corp
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Fuji Photo Film Co Ltd
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Publication date
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    • G—PHYSICS
    • G03—PHOTOGRAPHY; CINEMATOGRAPHY; ANALOGOUS TECHNIQUES USING WAVES OTHER THAN OPTICAL WAVES; ELECTROGRAPHY; HOLOGRAPHY
    • G03G—ELECTROGRAPHY; ELECTROPHOTOGRAPHY; MAGNETOGRAPHY
    • G03G13/00—Electrographic processes using a charge pattern
    • G03G13/26—Electrographic processes using a charge pattern for the production of printing plates for non-xerographic printing processes
    • G03G13/32—Relief printing plates
    • G—PHYSICS
    • G03—PHOTOGRAPHY; CINEMATOGRAPHY; ANALOGOUS TECHNIQUES USING WAVES OTHER THAN OPTICAL WAVES; ELECTROGRAPHY; HOLOGRAPHY
    • G03G—ELECTROGRAPHY; ELECTROPHOTOGRAPHY; MAGNETOGRAPHY
    • G03G9/00—Developers
    • G03G9/08—Developers with toner particles
    • G03G9/12—Developers with toner particles in liquid developer mixtures

Definitions

  • An electrophotographic liquid developer useful in converting an electrostatic latent image formed on an insulating surface into a visible or material image comprising a nonpolar, highly insulating carrier liquid and a toner powder which contains therein or absorbs a finely divided proteoiytic enzyme, or consists of a finely divided proteolytic enzyme, having a suitable polarity of charge dispersed in said carrier liquid.
  • a liquid developer for use in electrophotography generally I comprises a highly insulating, nonpolar organic liquid and electrostatically charged, finely divided particles dispersed therein, the former being sometimes referred to as the carrier liquid and the latter as the toner.
  • the liquid development method or electrophoretic development, is known to be capable of producing a developed image of the highest resolution and satisfactory tone reproduction mainly because the toner particles are stably dispersed in the carrier liquid as a far finer unit than in other developing materials, and because they deposit on a latent electrostatic image in the form of dispersed unit particles and not in agglomerated form.
  • the present invention relates to electrophotography wherein a toner is employed having a specific functionality.
  • a liquid developer of the present invention is characterized in that it contains a toner which comprises a proteolytic enzyme.
  • a master or matrix for printing or image duplication can be prepared by a quite simple operatron.
  • the present invention provides an electrophotographic liquid developer useful in converting an electrostatic latent image formed on an insulating surface into a visible or material image, comprising a nonpolar, highly insulating carrier liquid and a toner powder which contains therein or absorbs a finely divided proteolytic enzyme, or consists of a finely divided proteolytic enzyme, having a suitable polarity of charge dispersed in said carrier liquid.
  • the above-mentioned carrier liquid has an electric resistance or more than 10 ohm-cm. and a specific dielectric constant of less than 3.5.
  • FIG. I is a cross-sectional view of an electrophotographic recording member carrying on its light-sensitive surface a coating having a toner image containing a proteolytic enzyme (which will be hereinafter abbreviated as protease).
  • protease a proteolytic enzyme
  • l designates an electrophotographic recording member which comprises an electrically conductive support ll, and a photoconductive insulating layer 12.
  • the support is generally made of a material having a specific resistance lower than about 10 ohm-cm, suitable material including paper, metal plate, metallized paper or plastic films, etc.
  • the photoconductive insulating layer 12 may be of any type known in the art of electrophotography.
  • Typical examples of the photoconductive insulating coating are an amorphous selenium layer, zinc oxide/resin mixture layers, organic photoconductive layers, etc.
  • a toner image 2 contains therein a protease.
  • the area 3 is not covered with the toner.
  • the toner image may be provided by means of a typical xerographic process, which comprises charging in darkness of the photoconductive layer, image exposure of the charged surface, and development of the thus-produced latent electrostatic image by depositing the toner in sequence.
  • Other processes may also be employed to produce a toner image in the present invention, such as a Kallman process utilizing photoconductive aftereffect, or a thermoxerographic one in which an imagewise thermal radiation is used in place of visible light radiation.
  • FIG. 2 illustrates a procedure of matrix formation whereby the toner image-bearing recording member 1 is kept in an intimate contact with a matrix material 5 in the presence of sufficient moisture.
  • the matrix material 5 comprises a water-resistant backing 51 and a gelatin layer 52 coated thereon and having a thickness of several microns.
  • Suitable materials for backing 51 include films made of cellulose triacetate, polycarbonate, polyethyleneterephthalate, etc. or water-resistant paper.
  • the gelatin layer 52 may be colorless, but, for convenience of operation, it may also be intentionally dyed or made opaque by suitable materials.
  • the gelatin layer 52 may preferably be moistened, prior to contact with the enzyme image, and, at the same time, treated to have a desirable pH value,
  • the decomposition of gelatin is enhanced by heating the assembly to a temperature of from about 40 to 50 C.
  • the relief preparation is accompanied with less difiiculty as well as markedly decreased loss compared with those encountered in the relief preparation through tanning development.
  • Electrophotographic procedures requiring a toner image are simple, time saving, and economical.
  • Enzymes retain their catalytic activities when maintained in a dried condition, and likewise when they are dispersed in a nonpolar, carrier liquid which contains extremely little moisture.
  • the enzyn'ies which are employed in the present invention include those which originate in animals, such as pepsin, cathepsin, rennin, trypsin, chmstrypsin; plant protease such as bromelin, papin, chmypapin, ficin, asclepain; and bacteriotic protease such as Bacillus subtilis protease, etc.
  • Some of these enzymes such as papain, and ficin, require activators such as cystine, glutathione, or ascorbic acid for exertion of enzymetic activity.
  • activators such as cystine, glutathione, or ascorbic acid for exertion of enzymetic activity.
  • Such activators may be added to the liquid developer of the present invention.
  • enzymes Since enzymes have polypeptide chains in their molecular structure, they acquire an electrostatic charge of positive polarity when dispersed in an insulating carrier liquid. Therefore, fine particles of enzymes will be attracted to the charged area when applied on an electrostatic latent image of positive polarity, accomplishing attraction development, while, on the other hand, a repulsive or reversal development will occur with a latent image of negative polarity.
  • a liquid developer will be formulated so that the toner particles will mainly comprise a water-insoluble charge controlling resinous material and an enzyme as a minor ingredient in order to minimize lateral difi'usion of the enzyme during the intimate contact with a moistened gelatin coating.
  • charge controlling resinous material for use in electrophotographic liquid developers are described in many patent specifications (for example, U.S. Pat. No. 2,907,675; U.S. Pat. No. 3,078,231 and U.S. Pat. No. 3,198,649) or literature references already published, they will not be illustrated here.
  • an enzyme is incorporated in a charge controlling resinous material, the time required for decomposition of gelatin will be somewhat lengthened.
  • a liquid developer will result containing a toner of negative polarity, since the protease particles are absorbed on the surface of the polyvinylchloride powder by coulomb in teraction between charges of opposite polarities.
  • the size of the resinous toner particles containing or absorbing a protease is from 0.05 to microns.
  • the amount of the protease in the resinous toner is more than 0.05 percent by weight of the resinous toner, and more particularly from 0.2 to 5 percent by weight.
  • the amount of the protease in the developer ranges from 0.000005 to 0.25 percent by weight based on the carrier liquid.
  • the toners contained in the liquid developer of the present invention may consist of only finely divided protease particles, the size of the protease particles being from 0.01 microns to 5 microns.
  • suitable concentration of resinous toner in the liquid developer of the present invention is from 0.01 to 5 percent by weight of the carrier liquid.
  • suitable concentration of resinous toner in the liquid developer of the present invention is from 0.01 to 5 percent by weight of the carrier liquid.
  • ingredients such as unsaturated vegetable oils which impart a self-fixing property to the developed image may also be incorporated in the developers.
  • Stabilizers for enzymes may also be added. Further, it is suitable to stabilize the liquid developer by dissolving in the liquid developer a carrier liquid soluble resin such as long oil varnish, an alkyd resin. or a resinmodified phenol formaldehyde resin.
  • the above-mentioned carrier liquid soluble component may be added to the liquid developer of the present invention in an amount of from 0.2 to 30 percent by weight of the carrier liquid.
  • Suitable materials for the carrier liquid of the developers include aliphatic hydrocarbons, alicyclic hydrocarbons, aromatic hydrocarbons, halogenated hydrocarbons, polymethyl siloxane, etc.
  • EXAMPLE 1 One hundred mg. of a proteolytic enzyme purchased from Kaken Chemical Co., (located at Komagome, Bunkyo-ku, Tokyo) under the trade name Pronase P" was added into 150 ml. of purified kerosene, and subjected to supersonic agitation for several minutes. A homogeneous dispersion resulted. The dispersion was applied onto a zinc oxide electrophotographic paper, which had been charged and image-exposed, bearing an electrostatic latent image of negative polarity. Since the Pronase particles are positively charged, attraction development was accomplished.
  • a proteolytic enzyme purchased from Kaken Chemical Co., (located at Komagome, Bunkyo-ku, Tokyo) under the trade name Pronase P" was added into 150 ml. of purified kerosene, and subjected to supersonic agitation for several minutes. A homogeneous dispersion resulted. The dispersion was applied onto a zinc oxide electrophotographic paper,
  • EXAMPLE 2 lnto a mixture comprising ml. of cyclohexane and 50 ml. of k'erosene was dispersed 100 mg. of the same enzyme as was described in example 1. Then, 1 g. of resin-modified phenol-formaldehyde resin was dissolved in the liquid. In the dispersion the enzyme particles proved to assume a charge of positive polarity.
  • EXAMPLE 3 A liquid developer containing fine particles of polyvinyl chloride having a diameter of from 0.1 to 0.5 micron was prepared by supersonic agitation. This developer contained 0.2 percent of the toner by weight. To 1000 ml. of this developer was added 100 mg. of Pronase under supersonic agitation. A zinc oxide electrophotographic paper, bearing thereon an electrostatic latent image, was immersed in the resulting dispersion, whereby a repulsive development was accomplished due to the negatively charged dispersed particles. It was shown by the preparation of a gelatin relief employing this developed image that Pronase particles had deposited together with polyvinyl chloride particles on the sheet.
  • EXAMPLE 4 This example differs from example 3 only by the fact that 300 mg. of concentrated pepsin powder (dilution ratio 1:100) was substituted for the Pronase. Again it was proved that pepsin had been associated with polyvinyl chloride during electrophoretic behavior. Preparation of a gelatin relief was carried out in a low pH condition so as to raise the activity of the pepsin.
  • An electrophotographic liquid developer useful in converting an electrostatic latent image formed on an insulating surface into a visible or material image comprising a nonpolar, highly insulating, carrier liquid having an electric resistance of greater than 10 ohm-cm. and a specified dielectric constant of less than 3.5, and a resinous toner powder ranging in size from 0.05 to 10 microns, said toner powder containing therein a finely divided proteolytic enzyme at a level of from 0.000005 percent to 0.25 percent by weight based on the carrier liquid, having a suitable polarity of charge dispersed in said carrier liquid.
  • proteolytic enzyme is a member selected from the group consisting of pepsin, cathepsin, rennin, trypsin, hymotrypsin, bromelin, papin, chmspapin, ficin, asclepain, and Bacillus subtilis protease.
  • An electrophotographic liquid developer useful in converting an electrostatic latent image formed on an insulating surface into a visible or material image comprising a nonpolar, highly insulating, carrier liquid having an electric resistance of greater than 10' ohm-cm. and a specified dielectric constant of less than 3.5, and a resinous toner powder, said toner powder ranging in size from 001 to microns and being a finely divided proteolytic enzyme at a level of from 0.000005 percent to 0.25 percent by weight based on the carrier liquid, having a suitable polarity of charge dispersed in said carrier liquid.

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  • Physics & Mathematics (AREA)
  • General Physics & Mathematics (AREA)
  • Liquid Developers In Electrophotography (AREA)
  • Developing Agents For Electrophotography (AREA)
US819324A 1968-04-25 1969-04-25 Electrophotographic liquid developer having a proteolytic enzyme Expired - Lifetime US3622515A (en)

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JP2790068 1968-04-25

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US3622515A true US3622515A (en) 1971-11-23

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US (1) US3622515A (enrdf_load_stackoverflow)
BE (1) BE732124A (enrdf_load_stackoverflow)
DE (1) DE1920719A1 (enrdf_load_stackoverflow)
FR (1) FR2007520A1 (enrdf_load_stackoverflow)
GB (1) GB1231544A (enrdf_load_stackoverflow)
NL (1) NL6906325A (enrdf_load_stackoverflow)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3864125A (en) * 1969-02-10 1975-02-04 Xerox Corp Electrophotographic method of making an imaging master

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE4230142C1 (de) * 1992-09-09 1994-01-20 Kai Liebetruth Verwendung einer Übertragungsfolie

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US2742398A (en) * 1951-06-09 1956-04-17 Texaco Development Corp Method of removing deposits of wax and like materials
US2982692A (en) * 1957-06-26 1961-05-02 Hardin B Mcdill Dewaxing of oils
US3326771A (en) * 1963-12-12 1967-06-20 Mobil Oil Corp Enzymatic oxidation of hydrocarbons

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US2742398A (en) * 1951-06-09 1956-04-17 Texaco Development Corp Method of removing deposits of wax and like materials
US2982692A (en) * 1957-06-26 1961-05-02 Hardin B Mcdill Dewaxing of oils
US3326771A (en) * 1963-12-12 1967-06-20 Mobil Oil Corp Enzymatic oxidation of hydrocarbons

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3864125A (en) * 1969-02-10 1975-02-04 Xerox Corp Electrophotographic method of making an imaging master

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BE732124A (enrdf_load_stackoverflow) 1969-10-01
GB1231544A (enrdf_load_stackoverflow) 1971-05-12
FR2007520A1 (enrdf_load_stackoverflow) 1970-01-09
NL6906325A (enrdf_load_stackoverflow) 1969-10-28
DE1920719A1 (de) 1969-11-13

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