UNITED STATES PATENT AND TRADEMARK OFFICE
`
`BEFORE THE PATENT TRIAL AND APPEAL BOARD
`
`REACTIVE SURFACES LTD., LLP
`
`Petitioner
`
`TOYOTA MOTOR CORPORATION
`
`Patent Owner
`
`CASE: To Be Assigned
`
`Patent No. 8,394,618 B2
`
`DECLARATION OF DR. DAVID ROZZELL IN SUPPORT OF PETITION
`
`FOR INTER PAR TES REVIEW OF U.S. PATENT NO. 8,394,618 B2
`
`Reactive Surfaces Ltd., LLP Ex. 1010 — Page 1
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`TABLE OF CONTENTS
`
`Page
`
`INTRODUCTION ........................................................................................ .. 1
`
`SUMMARY OF OPINIONS ........................................................................ ..3
`
`QUALIFICATIONS AND EXPERIENCE .................................................. ..4
`
`A.
`
`B.
`
`C.
`
`Education and Work Experience ........................................................ ..4
`
`Compensation ................................................................................... .. 10
`
`Documents and Other Materials Relied Upon ................................. .. 10
`
`STATEMENT OF LEGAL PRINCIPLES ................................................. .. 10
`
`A.
`
`B.
`
`C.
`
`Claim Construction ........................................................................... .. 10
`
`Anticipation ...................................................................................... .. l I
`
`Obviousness ...................................................................................... .. l l
`
`LEVEL OF ORDINARY SKILL IN THE ART ........................................ .. 12
`
`TECHNOLOGY BACKGROUND OF CLAIMED SUBJECT
`MATTER OF THE ’61 8 PATENT. ........................................................... .. 13
`
`A.
`
`B.
`
`Disappearance of Fingerprints by Vaporization Occurs
`Without Enzyme ............................................................................... .. 13
`
`Inherent Enzymatic Functionality of Lipase is to Hydrolyze
`Lipids and Esters .............................................................................. .. 15
`
`Enzymatic Degradation of a Component of a Fingerprint
`
`by a Lipase Immobilized in or on a Substrate or Coating ................ .. 16
`
`Degradation of Components of a Fingerprint by a Lipase
`Makes the Components More Volatile and More Easily Vaporized .17
`
`Covalent Attachment to a Substrate or Coating Was Weli—Known
`at the Time of the Claimed Invention .............................................. ..18
`
`Non—Covalent Adherence to a Substrate or Coating Was
`Well—Known at the Time of the Claimed Invention ........................ .. 19
`
`The Selected Lipase Species Are Well—Known and Not Novel ...... ..20
`
`Many Polymeric Substrate/Coatings Have Been Used
`for Enzyme Immobilization or Association ..................................... ..20
`
`ii
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`TABLE OF CONTENTS
`
`VII. OVERVIEW OF THE ’618 PATENT ....................................................... ..21
`
`VIII. SUMMARY OF THE PRIOR ART ......................................................... .. 25
`
`IX.
`
`SUMMARY OF THE UNPATENTABILITY OPINIONS ...................... .. 35
`
`X.
`
`CLAIM CONSTRUCTION ....................................................................... ..36
`
`XI.
`
`UNPATENTABILITY OF THE ’618 PATENT CLAIMS ....................... ..44
`
`A.
`
`GROUND IA: CLAIMS 1-3 ARE
`
`UNPATENTABLE UNDER 35 U.S.C. § 103(A) As
`OBVIOUS OVER VAN ANTWERP .............................................. ..44
`
`GROUND 113: CLAIMS 4 AND 5 ARE
`
`UNPATENTABLE UNDER 35 U.S.C. § 103(A) AS
`OBVIOUS OVER VAN ANTWERP IN VIEW OF BOSTEK....... ..48
`
`GROUND 1C: CLAIMS 6-9 ARE
`
`UNPATENTABLE UNDER 35 U.S.C. § 103(A) AS
`OBVIOUS OVER VAN ANTWERP IN VIEW OF MOON .......... .. 51
`
`GROUND 1D: CLAIMS 10 AND 11 ARE
`
`UNPATENTABLE UNDER 35 U.S.C. § 103(A) AS
`OBVIOUS OVER VAN ANTWERP IN VIEW OF HAMADE ..... .. 54
`
`GROUND 2A: CLAIMS 1-8 AND 10-11 ARE
`
`UNPATENTABLE UNDER 35 U.S.C. § 103(A) AS
`OBVIOUS OVER SCHNEIDER .................................................... ..57
`
`GROUND 2B: CLAIM 9 IS UNPATENTABLE
`
`UNDER 35 U.S.C. § 103(A) AS OBVIOUS OVER
`SCHNEIDER IN VIEW OF MCDANIEL ....................................... ..65
`
`GROUND 3A: CLAIMS 1-9 ARE
`
`UNPATENTABLE UNDER 35 U.S.C. § 103(A) AS
`OBVIOUS OVER DREVON ........................................................... ..67
`
`GROUND 3B: CLAIMS 10 AND 11 ARE
`
`UNPATENTABLE UNDER 35 U.S.C. § 103(A) AS
`OBVIOUS OVER DREVON IN VIEW OF SCHNEIDER ............ ..74
`
`iii
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`TABLE OF CONTENTS
`
`ATTACHMENTS:
`
`A. Resume of Dr. David Rozzell
`B. “.-lnimobilization ofEnzymes by Covalent Attachment. ” Chapter 20 in
`“Methods in Biotechnology, Vol. 17: Microbial Enzymes and
`Biotransformations,” Ed. J. L. Barredo, Humana Press, Inc. Totowa, NJ,
`2005.
`. “Immobilization ofEnzymes: Techniques and Applications,” Chapter 13
`in “Biocatalytic Production of Amino Acids and Derivatives: New
`Developments and Process Considerations,” Eds. David Rozzel and Fritz
`Wagner, Hanser Publishers, 1992.
`. "Immobilized Aminotransferasesfor Amino Acid Production": J. David
`Rozzell., "Methods in Enzymology” Volume 136, Pages 479497, (1987)
`Immobilized Enzymes and Cells, Par’: C, lSBN:978-0—12—182036—7
`. Enzyme Nomenclature 1978, published in 1979, Academic Press, New
`York, pp. 234-239.
`. U.S. Patent 6,265,191
`. 1. "Optical resolution ofdl—menthol by entrappea’ biocatalysts": Saburo
`Fukui and Atsuo Tanaka, "Methods in Enzymology” Volume 136, Pages
`293-302, (1987) Immobilized Enzymes and Cells, Part C, ISBN:978—0—
`12—182036—7.;
`2. "lnalustrial operation of immobilized enzymes": l\/l.J. Daniels,
`"Methods in Enzymology” Volume 136, Pages 371-379, (1987)
`Immobilized Enzymes and Cells, Part C, ISBN:978—0—12—182036-7.;
`3. "Regiospecifc interesterification oftriglyceride with celite-adsorbed
`lipase": Shigeru Yamanaka and Takashi Tanaka, "Methods in
`Enzymology” Volume 136, Pages 405-411, (1987) Immobilized
`Enzymes and Cells, Part C, ISBN:978-0—12—182036—7.; and
`4. "Production ofaspartame by immobilized thermoase": Kiyotaka
`Oyama, Shigeaki Irino and Norio Hagi, "Methods in Enzymology”
`Volume 136, Pages 503-516, (1987) Iirimobilized Enzymes and Cells,
`Part C, ISBN:978—0~l2-18203 6-7
`
`iv
`
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`
`INTRODUCTION
`
`My name is J. David (“David”) Rozzell. For more than 2 decades, I have
`
`worked in the biotechnology industry with a specialization in the
`
`development of new enzymes and their applications.
`
`I currently work at
`
`Provivi, Inc. as Sr Vice-President of Biocatalysis, directing projects for the
`
`development of new enzymes and their use in the production of chemical
`
`compounds.
`
`I am also a founder and principle with Sustainable Chemistry
`
`Solutions, lnc., which is a consulting company and publisher of information
`
`products for the enzyme and biocatalysis markets.
`
`I am also co—founder and
`
`cunrent CEO of Catylix,
`
`Inc., a company developing new fluorination
`
`chemistry and its applications.
`
`Further details of my education, Work
`
`experience, selected publications, authored books, and patents on which I am
`
`an inventor are provided in my resume, which is Attachment A to this
`
`Declaration.
`
`I have been engaged to investigate and opine on certain issues relating to U.S.
`
`Patent No. 8,394,618 B2 entitled “LIPASE—CONTAINING POLYMERIC
`
`COATINGS FOR THE FACILITATED REMOVAL OF FINGERPRINTS
`
`(“the ’6l8 Patent” [Ex. 1001]) in Petition for Inter Partes Review of the ’6l8
`
`Patent (“the ’6l8 IPR Petition”) which requests the Patent Trial and Appeal
`
`Board (“PTAB”) to review and cancel Claims 1-11 of the ’6l 8 Patent.
`
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`I understand that, according to USPTO assignment records, the ’6l 8 Patent
`
`is owned by Toyota Motor Corporation.
`
`In this declaration, I will discuss the technology related to the ’6l8 Patent,
`
`including an overview of that technology as it was known prior to, and up to
`
`the time of the filing of U.S. application 12/820,063 (“the ‘G63 Application)
`
`from which the ’6l8 Patent issued. My understanding is that the earliest
`
`effective filing date of the’063 Application is June 21, 2010. This overview
`
`of the relevant technology provides some of the bases for my opinions with
`
`respect to the ’6l 8 Patent.
`
`This declaration is based on the information currently available to me. To
`
`the extent that additional information becomes available, I reserve the right
`
`to continue my investigation and study, which may include a review of
`
`documents and information that may be produced, as well as testimony from
`
`depositions that may not yet be taken.
`
`In forming my opinions, I have relied on information and evidence identified
`
`in this declaration, including the ’6l8 Patent, the prosecution history of the
`
`’6l8 Patent, and prior art references listed as Exhibits to the Petition for Inter
`
`Partes Review of the ’6l 8 Patent. I have also relied on my own experience
`
`and expertise in the relevant technologies and systems that were already in
`
`use prior to, and Within the timeframe of, the earliest effective filing date of
`
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`the claimed subject matter in the ’6l 8 Patent (i.e., June 21, 2010).
`
`II.
`
`SUMMARY OF OPINIONS
`
`7.
`
`The claims of the ’6l8 Patent are directed to technical issues or needs that
`
`were recognized and well understood, and technical solutions that were well
`
`developed to address the technical issues or needs, at the time of filing the
`
`application from which the ’6 l 8 Patent issued.
`
`For purpose of 1ny analysis in this declaration only and based on the
`
`disclosure and file history of the ’6l8 Patent, my understanding of certain
`
`terms in Claims 1-11 are discussed in detail in a laterpart of this declaration.
`
`In simple terms, Claims 1-11 of the ’6l 8 Patent attempt to claim a method of
`
`facilitating removal of a fingerprint from a substrate or a coating, which was
`
`is an inherent functionality of a substrate or coating having a lipase associated
`
`therewith. It is my opinion that the claims of the’6l8 Patent are rendered
`
`obvious by the prior art cited in the ’6l 8 IPR Petition in light of such inherent
`
`functionality of a lipase that is associated with a substrate or coating because
`
`there is nothing novel or non-obvious in such claims and because such claims
`
`merely recite routine and common limitations that were well known in the art
`
`before the filing date of the application from which the ’6l 8 Patent issued.
`
`The subsequent
`
`sections of this declaration will
`
`first provide my
`
`qualifications and experience and then describe details of my analysis,
`
`Reactive Surfaces Ltd., LLP Ex. 1010 - Page 7
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`

`
`observations and further opinions with respect to the Claims 1-11 of the ’61 8
`
`Patent.
`
`QUALIFICATIONS AND EXPERIENCE
`
`A.
`
`Education and Work Experience
`
`I obtained a Bachelor of Science degree in Chemistry in 1978 from the
`
`University of Virginia and a Ph.D. in Chemistry from Harvard University in
`
`1983. My dissertation was entitled: “Stereospecificity of Acetoacetate
`
`Decarboxylase. A New Synthesis of Chiral Methyl Acetate.”
`
`I have authored dozens of peer reviewed journal articles, several chapters in
`
`books, and given numerous presentations at symposia around the world in the
`
`field of enzymes, biocatalysis, and organic chemistry. (See relevant sections
`
`of Attachment A).
`
`I currently serve as Sr. Vice—President, Biocatalysis, at Provivi, Inc. in Santa
`
`Monica, CA. I joined Provivi, Inc. in 2015 with the responsibility of leading
`
`development and commercialization of novel enzymes catalyzing the
`
`synthesis of chiral cyclopropanes via a carbene transfer mechanism. My
`
`specific responsibilities include managing internal R & D, business
`
`development, customer acquisition and project management to meet rigorous
`
`timelines for development-.
`
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`4
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`14.
`
`I currently also serve as CEO and Founder of Sustainable Chemistry
`
`Solutions, Inc., in Burbank, CA. Through Sustainable Chemistry Solutions,
`
`Inc., I am the publisher of the web site http://www.bio—catalyst.com, which
`
`provides information and insights on ‘oiofuels, bi0—based chemicals, and
`
`biocatalysis and am also the publisher ofmonthly newsletter Enzyme Industry
`
`Newsletter, offering information products and consulting services related to
`
`enzymes and biocatalysis to pharmaceutical and chemical companies.
`
`I
`
`provide consulting support
`
`to programs for the development of novel
`
`enzymes and their applications, and also for pathways in bio—based chemical
`
`production.
`
`I am creator and publisher of the Enzyme Company Guide and
`
`the Biocatalysis Company Guide, providing business and technical
`
`information to industry specialists. I also offer expert witness services in
`
`patent litigation and cases involving enzymes and the development and
`
`enzyme—based processes and applications.
`
`Since 2011, I have served as CEO and Co—Founder of Catylix, Inc.
`
`in
`
`Burbank, CA. Together with the other co—founder, we established this
`
`company to develop and commercialize a novel, broadly—useful chemistry for
`
`adding fluorine—containing functional groups to chemical compounds. Our
`
`first product called Trifluoromethylator® was launched in July 2011. The
`
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`
`main product applications are in the discovery of pharmaceuticals and crop
`
`protection agents with improved efficacy and metabolic stability.
`
`I served as President and CEO of Solidus Biosciences, Inc. in San Francisco,
`
`CA from 2009 to 2010.
`
`In leading this company, which was developing a
`
`novel, chip-based in vitro toxicology platform,
`
`I was responsible for
`
`managing company operations, setting business strategy, developing new
`
`customer relationships, and raising funds from investors.
`
`From 2007 to 2008,
`
`I served as VP, Biocatalysis Technology and
`
`Applications for Codexis, Inc. following its acquisition of BioCatalytics, Inc.
`
`in July 2007. I was responsible for the identification and development of new
`
`technologies,
`
`including technologies developed and in—licensed through
`
`external collaborati_ons.
`
`I managed a network of external collaborations in
`
`the USA and Europe, promoting the company and supporting business
`
`development activities through technical presentations, press conferences,
`
`and written articles. I also initiated an emphasis on Green Chemistry.
`
`I was Founder, President, CS0 and CEO at BioCatalytics, Inc. in Pasadena,
`
`CA from 1996 to 2007. 1 established this biotechnology company to develop
`
`and commercialize enzymes and enzyme-based processes for the production
`
`of optically active pharmaceutical
`
`intermediates and other
`
`specialty
`
`chemicals. 1 built this company into a profitable seller of novel enzymes for
`
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`6
`
`

`
`chemical synthesis, with one of the world’s largest enzyme product lines.
`
`I
`
`established a European office in 2005 and a subsidiary BioCatalytics Europe
`
`Gmbl-I in Graz, Austria in 2006. BioCatalytics, Inc. was acquired in 2007 by
`
`Codexis, Inc.
`
`I was Co—Founder and Acting CEO of EraGen Biosciences, Inc. (initially
`
`established as Sulfonics, Inc.) in Madison, WI from 1994-1996. I co—founded
`
`this start—up biotechnology company, which focused on applications of non-
`
`standard nucleic acid bases and protein structure prediction. This company
`
`raised seed capital from individual investors and the Novartis Venture Fund.
`
`I acted as CEO until a full-time person was recruited to establish the company
`
`in its first headquarters in Florida.
`
`During my time with Exogene Corporation in Monrovia, CA, I first served
`
`as Vice-President of Research & Development (1991-1992) and then as
`
`President (1992-1994). My responsibilities included business development,
`
`negotiation of sponsored research and technology licensing agreements,
`
`general scientific guidance of the company's research, and supervision of the
`
`administrative and senior scientific staff.
`
`I served as Director of Research and Biotreatrnent Systems at Celgene
`
`Corporation in Warren, NJ from 1988-1991. This company employed a
`
`combination of biocatalytic
`
`reactions
`
`and organic
`
`chemistry. My
`
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`7
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`responsibilities included directing both proprietary and collaborative research
`
`programs focused on the production of pharmaceutical intermediates and
`
`specialty chemicals and in the biocatalytic degradation of environmentally-
`
`hazardous chemicals in waste streams.
`
`During my time with Genetics Institute, Inc. in Cambridge, MA, I first served
`
`as Senior Scientist (1983-1986) and then as Director of Biocatalysis Research
`
`(1986-1988). I built and managed an interdisciplinary group of professionals
`
`and directed the research and development activities of an Applied
`
`Enzymology group and a Biocatalysis group. My efforts in these positions
`
`resulted in more than $1 million in revenues through funding and license
`
`agreements, and the commercialization of processes to manufacture optically
`
`active amino acids at the multi—hundred ton per year scale.
`
`With respect to the claimed invention, I have specific experience in the areas
`
`of the cloning and expression of genes encoding enzymes, the improvement
`
`of enzymes through directed evolution methods,
`
`the use of enzymes to
`
`catalyze various chemical reactions, and the immobilization of enzymes on
`
`polymeric materials and surfaces by either covalent or non—covalent means.
`
`In my previous research work, I have immobilized various types of enzymes,
`
`including
`
`lipases,
`
`proteases,
`
`amidases,
`
`esterases,
`
`oxidoreductases,
`
`transaminases, and other enzymes on various types of materials. This work
`
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`8
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`

`
`includes specific examples of immobilization by both covalent (chemical
`
`bonding) and non—covalent (adsorption, entrapment in a polymeric gel or
`
`coating) methods. In one case, I adsorbed lipases from different sources onto
`
`cross-linked
`
`polystyrene
`
`and
`
`polyacry1ate—co-polymers
`
`for use
`
`in
`
`hydrolyzing or transesterifying esters. I have also immobilized enzymes by
`
`entrapment in gels formed by the condensation of polymers such as chitosan
`
`calcium alginate, and kappa—carrageenan, or by entrapment within gels
`
`formed by a polymerization or curing process, such as the polymerization of
`
`polyacrylamide. I have also immobilized enzymes onto materials such as
`
`silica or alumina which have had their surfaces chemically modified or coated
`
`with an organic compound or polymer.
`
`I have also published articles about enzyme immobilization. I was a co—author
`
`of a book chapter describing methods of covalent enzyme immobilization
`
`entitled “Immobilization of Enzymes by Covalent Attachment.” This was
`
`published as chapter 20 in “Methods in Biotechnology, Vol. 17: Microbial
`
`Enzymes and Biotraiisformations,” edited by J. L. Barredo and published by
`
`Humana Press, Inc. Totowa, NJ. (Attachment B) I am also the author of
`
`“Immobilization of Enzymes: Techniques and Applications” published as
`
`Chapter 13 in the book “Biocatalytic Production of Amino Acids and
`
`Derivatives: New Developments and Process Considerations,” published by
`
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`9
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`
`Hanser Publishers in 1992 (Attachment C). I also have written about my
`
`research on the use of immobilized Transaminases for the production of
`
`amino acids [see, for example, "Immobilized Aminotransférases for Amino
`
`A Cid Production" : J. David Rozzell, "Methods in Enzymology” Volume 13 6,
`
`Pages 479-497, (1987) Immobilized Enzymes and Cells, Part C, ISBN:978—
`
`0—12—l82036-7.] (Attachment D).
`
`B.
`
`Compensation
`
`My services in this matter, which are being provided through Sustainable
`
`Chemistry Solutions, Inc, whose offices are located at 437 South Sparks
`
`Street, Burbank, California 91506, are being compensated at a rate of $375
`
`per hour. This compensation is not contingent upon my performance, the
`
`outcome of this inter partes review or any other proceeding, or any issues
`
`involved in or related to this inter partes review.
`
`C.
`
`Documents and Other Materials Relied Upon
`
`The documents on which I rely for the opinions expressed in this declaration
`
`are documents and materials identified in this declaration, including the ’618
`
`Patent, any related patents and applications in the same family as the ’6l8
`
`Patent, the prosecution history for the ’618 Patent and that of any related
`
`family members of the ’618 Patent,
`
`the cited prior art references and
`
`associated information discussed in this declaration, and any other references
`
`Reactive Surfaces Ltd., LLP Ex. 1010 - Page 14
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`10
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`
`specifically identified in this declaration,
`
`in their entirety, even if only
`
`portions of these documents are discussed here in an exemplary fashion.
`
`STATEMENT OF LEGAL PRINCIPLES
`
`A.
`
`Claim Construction
`
`Iunderstand that, when construing claim terms, a claim subj ect to interpartes
`
`review receives the “broadest reasonable construction in light of the
`
`specification of the patent in which it appears.” I further understand that the
`
`broadest reasonable construction is the broadest reasonable interpretation
`
`(“BRI”) of the claim language, and that any term that lacks a definition in the
`
`specification is also given a broad interpretation.
`
`B.
`
`Anticipation
`
`I understand that in order for a patent claim to be valid, the claimed invention
`
`must be novel. I further understand that if each and every element of a claim
`
`is disclosed in a single prior art reference, then the claimed invention is
`
`anticipated, and the invention is not patentable according to pre-AIA 35
`
`U.S.C. § 102 effective before March 16, 2013. I also understand, in order for
`
`the invention to be anticipated, each element of the claimed invention must
`
`be described or embodied, either expressly or inherently, in the single prior
`
`art reference. It is also my understanding that, in order for a reference to
`
`inherently disclose a claim limitation, that claim limitation must necessarily
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`Reactive Surfaces Ltd., LLP Ex. 1010 - Page 15
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`ll
`
`

`
`be present in the reference. I also understand that a prior art reference must
`
`be enabling in order to anticipate a patent claim.
`
`C.
`
`Obviousness
`
`I understand that obviousness under pre-AIA 35 U.S.C. § 103 effective before
`
`March 16, 2013 is a basis for invalidity. Specifically, Iunderstand that where
`
`a prior art reference discloses less than all of the limitations of a given patent
`
`claim, that patent claim is invalid if the differences between the claimed
`
`subject matter and the prior art reference are such that the claimed subject
`
`matter as a whole would have been obvious at the time the invention was
`
`made to a person having ordinary skill in the relevant art (“POSITA”). It is
`
`also my understanding that obviousness can be based on a single prior art
`
`reference or a combination of references that either expressly or inherently
`
`disclose all limitations of the claimed invention.
`
`LEVEL OF ORDINARY SKILL IN THE ART
`
`I understand that the claims and specification of a patent must be read and
`
`construed through the eyes of a POSITA at the time of the earliest effective
`
`filing date of the application from which the patent issued. 1 also understand
`
`that to determine the appropriate level of a POSITA, the following factors
`
`may be considered: (a) the types of problems encountered by those Working
`
`in the field and prior art solutions thereto; (b) the sophistication of the
`
`Reactive Surfaces Ltd., LLP Ex. 1010 — Page 16
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`12
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`technology in question, and the rapidity with which innovations occur in the
`
`field; (c) the educational level of active workers in the field; and (d) the
`
`educational level of the inventor.
`
`Based on the above considerations and factors, it is my opinion that a person
`
`having ordinary skill in the art would have at least a bachelor’s degree plus 5
`
`or more years of experience, or a Masters or PhD degree with 2 or more years
`
`of experience in chemistry, biochemistry, molecular biology, biochemical
`
`engineering, or a related discipline. This description is approximate and
`
`additional years of experience can compensate for less formal education in a
`
`discipline, and a POSITA could have combined experience in more than one
`
`of the disciplines listed above.
`
`TECHNOLOGY BACKGROUND OF CLAIMED
`
`SUBJECT MATTER OF THE ’618 PATENT
`
`A.
`
`Disappearance of Fingerprints by Vaporization Occurs Without
`Enzyme
`
`As an initial matter, it is important to understand that it is well—established
`
`that fingerprints disappear from surfaces over time without having been
`
`contacted with an enzyme such as a lipase, and that the mechanism of this
`
`disappearance is by vaporization.
`
`Buchanan [Ex. 1013] studied fingerprints from about 50 individuals ranging
`
`in age from 3
`
`to 64 years,
`
`the fingerprints were analyzed for their
`
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`13
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`
`compositions by gas chromatography to characterize,
`
`in particular,
`
`the
`
`volatility of the components. In general, the author found that samples
`
`obtained from children contained more volatile fatty acids, esters, and related
`
`compounds, and samples from adults contained less volatile fatty acids,
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`esters, and related compounds, providing a differentiating characteristic
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`between the fingerprints of adults and children that could be useful in solving
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`crimes. (Id. at Abstract:l—8) In a real~world test of these laboratory results,
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`the author further found that fingerprints deposited by children in vehicles
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`disappeared in less than 24 hours; fingerprints from adults lasted at least
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`several days. No treatments of any kind were applied to the fingerprints to
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`facilitate their disappearance. The author further found that when fingerprints
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`were subjectedto mild heating (allowing the vehicle to sit in sunlight in the
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`summer), the rate of their disappearance was faster, (Id. at 89:21~29) as would
`
`be expected from a vaporization mechanism in my opinion. Buchanan thus
`
`concluded that
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`fingerprints and their components can disappear by
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`vaporization, and that
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`this vaporization would occur under ambient
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`conditions or with mild heating, and that fingerprints containing more volatile
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`components vaporized more quickly than fingerprints containing a lower
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`amount of volatile components. (Id. at 91 :1-7)
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`Given that Buchanan demonstrates that a fingerprint or a similar mark or stain
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`14
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`on a surface will become less visually apparent over time, and that the
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`mechanism of its disappearance is by vaporization, it is my opinion that it
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`would be obvious to_a POSITA that fingerprints can be removed from a
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`surface, substrate or coating by vaporization, and that the disappearance by
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`vaporization would occur whether or not the fingerprint has been in contact
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`with an enzyme such as a lipase. In my opinion it is an inherent property of
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`fingerprints that they would disappear from a surface by vaporization.
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`Reading of Buchanan (e.g., Id. at 89:21-29; 91:1—7) would make it further
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`obvious to a POSITA that fingerprints containing more volatile (i.e. lower
`
`molecular weight) components would disappear by vaporization more
`
`quickly.
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`B.
`
`Inherent Enzymatic Functionality of Lipase is to Hydrolyze
`Lipids and Esters
`
`It is well—known that lipases in general will hydrolyze, and thereby degrade,
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`various lipid—based compounds. Lipases will degrade triglycerides and other
`
`lipids, wax esters, other fatty acid esters, cholesterol esters, and similar
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`compounds, which are well-known to be among the components of
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`fingerprints (see, for example, Buchanan at Abstractcl-8; 90:31 to 91:19). In
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`fact, the ‘618 Patent states that these types of compounds are well—known to
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`be present in fingerprints and similar stains (‘618 Patent at 2:38-48), and that
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`15
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`lipases are well-known to degrade these types of compounds (Id. at 2:34-37,
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`2:43-48). Indeed, hydrolyzing various types of lipids and fatty acid esters is
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`a defining characteristic of a lipase and an inherent property of lipases in
`
`general. For example, the products of a triacylglycerol lipase’s enzymatic
`
`action on a triacylglycerol lipid as would be found in a fingerprint produces
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`glycerols and fatty acids. [See , Attachment E; Enzyme Nomenclature 1978,
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`published in 1979, Academic Press, New York, pp. 234~239].
`
`Further, a lipase non—covalently immobilized on a surface has also been
`
`described, in which the lipase was absorbed onto a fabric surface to facilitate
`
`removal of an oil stain (See Attachment F, US. Patent 6,265,191, at 6: 5—
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`8:50).
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`In my opinion,
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`it would be an inherent property that a lipase
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`immobilized on a surface would degrade a triglyceride—based oil stain.
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`Therefore, in my opinion, it is unsurprising and completely expected that a
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`lipase would degrade lipid and ester components of a fingerp1'int, and
`
`therefore the degradation of fingerprint components by a lipase would have
`
`been obvious to a POSITA at the time of the invention.
`
`C.
`
`Enzymatic Degradation of Components of a Fingerprint by a
`Lipase Immobilized in or on a Substrate or Coating
`
`38.
`
`The materials described in the ‘6l 8 patent are Various substrates or coatings
`
`that have‘ a lipase enzyme adsorbed, covalently attached, or otherwise
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`Reactive Surfaces Ltd., LLP Ex. 1010 - Page 20
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`16
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`adhered to or entrapped in that substrate or coating. (Id. at 7:26-39, 8:13-18,
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`8:39-46, 15:30-32) Such materials are well—known in the art. (See Sections
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`V103) and (F) in this declaration for a more detailed explanation.) It has also
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`been shown in many cases and with many different materials, including
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`substrates and coatings such as those described in the ‘618 patent,
`
`that
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`catalytic activity of the lipase is typically retained on immobilization in or on
`
`the substrate or coating. As such, the substrates or coatings with lipases
`
`attached or adhered thereto as described in the ‘6l8 patent are similar, if not
`
`identical, to numerous other immobilized lipase materials that have been
`
`prepared and described in the prior art. Juxtaposing the description of lipases
`
`immobilized in or on a surface, polymer, substrate, or coating as provided in
`
`the ‘GIS patent with the vast amount of prior art describing lipases
`
`immobilized in or on similar surfaces, polymers, substrates, or coatings [See,
`
`for example, Attachment G;
`
`1. "Optical resolution of dl-mentlvol by
`
`entrapped l7i0caralysl‘s": Saburo Fukui and Atsuo Tanaka, "Methods in
`
`Enzymology” Volume 136, Pages 293-302, (1987) Immobilized Enzymes
`
`and Cells, Part C, lSBN:978-0—l2—l82036-7.; 2. "Industrial operation of
`
`immobilized enzymes": M.J. Daniels, "Methods in Enzymology” Volume
`
`136, Pages 371-379,
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`(1987) Immobilized Enzymes and Cells, Part C,
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`ISBN:978-0-l2-l82036—7.;
`
`3.
`
`"Regiospecific
`
`imferesterification
`
`of
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`Reactive Surfaces Ltd., LLP Ex. 1010 ~ Page 21
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`17
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`triglyceride with celite—ads0rbed lipase": Shigeru Yamanaka and Takashi
`
`Tanaka, "Methods in Enzymology” Volume 136, Pages 405-411, (1987)
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`Immobilized Enzymes and Cells, Part C, lSBN:978-0-12-182036-74 and 4.
`
`"Production of aspartame by immobilized thermoase": Kiyotaka Oyama,
`
`Shigeaki Irino and Norio Hagi, "Methods in Enzymology” Volume 136,
`
`Pages 503-516, (1987) Immobilized Enzymes and Cells, Part C, ISBN:978-
`
`0—l2—l82036—7”], we have an direct comparison of lipase—associated
`
`materials and their functionality.
`
`Because a lipase immobilized on or within a surface, polymer, substrate, or
`
`coating would be expected to retain at least some of its inherent activity to
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`hydrolyze various ester and lipid components such as those components
`
`found in a fingerprint, in my opinion it would have been obvious to a POSITA
`
`at the time of the invention to employ a lipase immobilized in or on a coating
`
`as described iii the ‘6l 8 patent for the purpose of degrading one or more lipid
`
`components of a fingerprint.
`
`D.
`
`Degradation of Components of 3 Fingerprint by a Lipase Makes
`the Components More Volatile and More Easily Vaporized
`
`Buchanan described the analysis of fingerprints of adults and children by gas
`
`chromatography, showing that the fingerprints of children have more volatile
`
`components than the fingerprints of adults, and are therefore more readily
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`18
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`Vaporizable and disappear more quickly. (Buchanan at Abstractzl-8, 89:21—
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`29; 91 : 1-7). Thus, one or more of the components of fingerprints will
`
`disappear without the presence of a lipase associated substrate or coating as
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`described in the ‘61 8 patent.
`
`Lipase—catalyzed degradation of lipid substances, such as those known to be
`
`components of fingerprints, break these components down into compounds
`
`of lower molecular weight and generally higher volatility. Thus, the inherent
`
`activity of a lipase to break down lipid