Trials@uspto.gov
`571.272.7822
`
`
`Paper 10
`Date: May 17, 2021
`
`
`UNITED STATES PATENT AND TRADEMARK OFFICE
`____________
`
`BEFORE THE PATENT TRIAL AND APPEAL BOARD
`____________
`
`DANISCO US INC. and DUPONT NUTRITION BIOSCIENCES ApS,
`Petitioner,
`
`v.
`
`NOVOZYMES A/S,
`Patent Owner.
`____________
`
`IPR2021-00188
`Patent 10,058,107 B2
`____________
`
`
`
`Before JAMES A. WORTH, ROBERT A. POLLOCK, and
`RYAN H. FLAX, Administrative Patent Judges.
`
`FLAX, Administrative Patent Judge.
`
`
`
`
`DECISION
`Granting Institution of Inter Partes Review
`35 U.S.C. § 314
`
`
`
`
`
`

`

`IPR2021-00188
`Patent 10,058,107 B2
`
`
`Danisco US Inc. and DuPont Nutrition Biosciences ApS (collectively
`“Petitioner”) filed a Petition for an inter partes review of claims 1, 3–9, and
`11–17 of U.S. Patent 10,058,107 B2 (“the ’107 patent,” Ex. 1001). Paper 1
`(“Pet.”). Novozymes A/S (“Patent Owner”) filed a Preliminary Response.
`Paper 9 (“Prelim. Resp.”).
`Under 37 C.F.R. § 42.4(a), we have authority to determine whether to
`institute trial in an inter partes review. We may institute an inter partes
`review if the information presented in the petition filed under 35 U.S.C.
`§ 311, and any preliminary response filed under § 313, shows that there is a
`reasonable likelihood that Petitioner would prevail with respect to at least
`one of the claims challenged in the petition. 35 U.S.C. § 314.
`After reviewing the parties’ submissions, we conclude Petitioner
`demonstrates a reasonable likelihood it would prevail in showing that claims
`of the ’107 patent are unpatentable under the presented ground. Therefore,
`we institute inter partes review of all challenged claims (1, 3–9, and 11–17)
`under the ground raised in the Petition, pursuant to 35 U.S.C. § 314. See
`SAS Inst., Inc. v. Iancu, 138 S. Ct. 1348, 1359–60 (2018); see also Guidance
`on the Impact of SAS on AIA Trial Proceedings (April 26, 2018) (available
`at https://www.uspto.gov/patents-application-process/patent-trial-and-
`appeal-board/trials/guidance-impact-sas-aia-trial) (“Guidance”).
`INTRODUCTION
`I.
`A. REAL PARTIES-IN-INTEREST
`Petitioner identifies “Danisco US Inc., DuPont Nutrition Biosciences
`ApS, and International Flavors & Fragrances Inc.” as real parties-in-interest.
`Paper 8. Patent Owner identifies “Novozymes A/S, Novozymes North
`America Inc. and Chr. Hansen A/S” as real parties-in-interest. Paper 6.
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`IPR2021-00188
`Patent 10,058,107 B2
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`B.
`
`RELATED MATTERS
`Petitioner identifies IPR2021-00189 regarding U.S. Patent 10,555,541
`as a related matter. Pet. 4 (“The claims of the ’541 patent are nearly
`identical to the claims of the ’107 patent, differing only by the added
`requirement that the claimed polypeptide is ‘isolated.’”). Patent Owner
`identifies the same proceeding as a related matter. Paper 6.
`THE ’107 PATENT
`C.
`The ’107 patent is titled “METHOD FOR PRODUCING A DAIRY
`PRODUCT.” Ex. 1001, code (54). The ’107 patent issued on August 28,
`2018, from U.S. Application 15/433,642 (“the ’642 application,” see
`Ex. 1011), which was filed on February 15, 2017, and claims priority as a
`continuation to U.S. Application 12/744,508 (“the ’508 application”), which
`was originally filed on December 2, 2008 as international application
`PCT/EP2008/066624 (“the ’624 PCT application”), and also claims priority
`to U.S. Provisional Application 61/055,164 filed May 22, 2008, U.S.
`Provisional Application 60/992,783 filed December 6, 2007, European
`Application 07122110.5 filed December 3, 2008, and European Application
`08156674.7 filed May 21, 2008.1 Ex. 1001, codes (45), (21), (63), (60),
`(30), 1:7–17.
`
`
`1 Petitioner challenges the ’107 patent’s claim to priority to any date earlier
`than the patent’s actual filing date of February 15, 2017. Pet. passim. Patent
`Owner identifies the ’107 patent’s claim to priority to each of the identified
`preceding filings, but also states that “the challenged claims are entitled to at
`least the December 2, 2008, filing date of the ʼ624 PCT,” and that “[f]or
`purposes of the IPR and the prior art status of Larsen, it is not necessary to
`reach the issue of whether the ʼ107 patent claims are entitled to the earlier
`filing dates of these applications.” Prelim. Resp. 3–4, n.2, 19.
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`IPR2021-00188
`Patent 10,058,107 B2
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`
`The ’107 patent’s Abstract states: “The present invention relates to a
`method for producing a dairy product using an enzyme having lactase
`activity.” Id. at Abstract. The ’107 patent further states that “to help dairy
`maldigesters keep dairy foods in their diet, there is a growing demand for
`dairy food products that contain no or only low levels of lactose,” and
`“[l]actase is used commercially to break down lactose in milk to produce
`dairy products which are suitable for people with lactose intolerance and/or
`have a sweeter taste.” Id. at 1:34–39. Further, the ’107 patent states “[a]
`lactase from Bifidobacterium bifidum has been described having a high
`transgalactosylating activity, both in the full-length form and especially
`when truncated from the C-terminal end (see, e.g., Jørgensen et al. (2001),
`Appl. Microbiol. Biotechnol., 57: 647-652 or EP patent 1,283,876),” and
`“[i]t is an object of the present invention to provide a method for production
`of dairy products, e.g. fermented dairy products, such as yoghurt, having a
`low level of lactose by using a lactase,” thus “[l]actase to be used according
`to the invention should hydrolyse lactose efficiently and optimally allow for
`almost complete lactose hydrolysis. Especially, such lactase should have a
`high ratio of lactase to transgalactosylase activity.” Id. at 2:8–26.
`Regarding this interplay between lactase hydrolyzing and
`transgalactosylating functionality, the ’107 patent states
`The present inventors have surprisingly found that a C-
`terminally truncated fragment of the extracellular lactase from
`Bifidobacterium bifidum, which was originally isolated and
`patented for its ability to make high amounts of
`galactooligosaccharides from lactose, can be used very
`successfully for hydrolysis of lactose in milk. When tested in
`water+100 g/l lactose at 37 °C., the enzyme makes
`galactooligosaccharides with high efficiency as described in the
`prior art. However, when tested in milk, the ratio of hydrolytic
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`IPR2021-00188
`Patent 10,058,107 B2
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`
`to transgalactosylating activity has changed markedly, resulting
`in efficient hydrolysis and very low production of
`galactooligosaccharides.
`Id. at 2:32–43. The ’107 patent explains that “[a] lactase in the context of
`the present invention is any glycoside hydrolase having the ability to
`hydrolyse the disaccharide lactose into constituent galactose and glucose
`monomers,” but that “[a] lactase in the context of the invention may have
`other activities than the lactose hydrolysing activity, such as for example a
`transgalactosylating activity.” Id. at 11:32–41.
`The ’107 patent identifies many organisms from which a lactase
`enzyme may be derived, but describes that one preferred enzyme is a lactase
`from the bacteria species Bifidobacterium bifidum
`having a sequence which is at least 50%, such as at least 60%,
`at least 70%, at least 80%, at least 90%, at least 95% or at least
`98% identical to amino acids 28-1931 of SEQ ID NO: 1 or to a
`lactase active fragment thereof. Such lactase active fragment of
`SEQ ID NO: 1 may be any fragment of SEQ ID NO: 1 having
`lactase activity. A lactase active fragment of SEQ ID NO: 1
`may be, e.g., amino acids 28-979, amino acids 28-1170, amino
`acids 28-1323, amino acids 28-1331, or amino acids 28-1600 of
`SEQ ID NO: 1.
`Id. at 11:50–12:25. Other than the claims, this is the only mention in the
`’107 patent of the amino acid sequence 28–979 of SEQ ID NO: 1 and no
`smaller fragments of this amino acid sequence are identified. See generally
`id.; see also id. at col. 23–33 (SEQ ID NO: 1); see also Pet. 19 (citing
`Ex. 1002 ¶¶ 62–63, and noting this singular disclosure).
`The ’107 patent describes that in one
`preferred embodiment, the enzyme when hydrolysing the
`lactose in the milk-based substrate has a ratio of lactase to
`transgalactosylase activity of more than 1:1, such as more than
`2:1 or more than 3:1. In another preferred embodiment, the
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`
`enzyme treatment is performed under conditions where the
`lactase activity of the enzyme is higher than the
`transgalactosylase activity, such as at least two times higher or
`at least three times higher.
`Ex. 1001, 15:39–46. And, “[i]n another preferred embodiment, the enzyme
`treatment is performed under conditions where the hydrolyzed lactose is
`converted into equal amounts of free glucose and free galactose.” Id. at
`15:51–54.
`The ’107 patent also includes disclosures of ten examples indicated to
`embody the invention or exemplify a known lactase enzyme (i.e., Lactozym,
`a commercially available lactase from Novozymes A/S) to provide a
`comparison. See id. at 15:55–24:47 (Examples 1–10). In these examples, in
`each reported testing of an experimental lactase, the enzyme was derived
`from Bifidobacterium bifidum and had the amino acid sequence shown in
`SEQ ID NO: 2, which is not the amino acid 28–979 fragment of SEQ ID
`NO: 1, and, in each instance where measured, the experimental lactase
`produced galactose and glucose in equal amounts, which indicates no
`galactose was transferred to produce galactooligosaccharides (GOS). Id.;
`see also id. at 24:39–44 (explaining that when using the experimental lactase
`having an amino acid sequence as shown in SEQ ID NO: 2 glucose and
`galactose were produced equally, but the use of “Lactozym produces less
`galactose than glucose clearly showing that galactooligosaccharides have
`been produced,” i.e., that transgalactosylation occurred); see also Pet. 20–22
`(citing Ex. 1002 ¶¶ 48–53, and discussing these examples and noting the
`lack of transgalactosylation).
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`IPR2021-00188
`Patent 10,058,107 B2
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`
`CLAIMS CHALLENGED
`1, 3–9, 11–17
`
`35 U.S.C. §2
`103
`
`The ’107 patent includes independent claims 1 and 11, which state:
`1. A polypeptide having transgalactosylating activity,
`which is a truncated polypeptide consisting of the amino acid
`sequence of amino acids 28-979 of SEQ ID NO: 1 or is a
`fragment thereof having transgalactosylating activity.
`11. A polypeptide having transgalactosylating activity,
`which is a fragment having an amino acid sequence which is at
`least 98% identical to amino acids 28-979 of SEQ ID NO: 1,
`wherein the fragment consists of at most 952 amino acid
`residues and has transgalactosylating activity.
`Id. at 83:13–16, 84:15–19. In addition to independent claims 1 and 11, the
`’107 patent includes dependent claims 2–10 and 12–17, each set respectively
`depending from the preceding independent claim and more specifically
`defining aspects of the claimed polypeptide or a method of forming such a
`polypeptide or a product incorporating such a polypeptide. Id. at 83:17–35,
`84:12–14, 84:20–33 (claims 2 and 10 are not challenged in this proceeding).
`PETITIONER’S ASSERTED GROUND FOR UNPATENTABILITY
`D.
`Petitioner asserts one ground for the unpatentability of claims 1, 3–9,
`and 11–17 of the ’107 patent:
`
`
`REFERENCE(S)/BASIS
`Larsen3
`
`
`
`2 Petitioner asserts that the ’107 patent has a priority date of February 15,
`2017, which is after the AIA revisions to 35 U.S.C. § 103 (and § 112) took
`effect. Patent Owner asserts that the ’107 patent has a priority date at least
`as early as December 2, 2008, which is before the AIA took effect.
`Regardless of whether the pre- or post-AIA version of the Patent Act
`applies, the same substantive legal requirements apply and no change in the
`law impacts the outcome of this Decision.
`3 US 2015/0223481 A1 (published Aug. 13, 2015) (Ex. 1003, “Larsen”).
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`Patent 10,058,107 B2
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`See Pet. 6. In support of this ground for unpatentability Petitioner submits,
`inter alia, the Declaration of Douglas S. Clark, Ph.D. Ex. 1002. At this
`stage of the proceeding, we determine that Dr. Clark is qualified to offer
`testimony on the knowledge of one of ordinary skill in the art (for any
`potential priority date for the ’107 patent). See, e.g., id. ¶¶ 3–38, 43
`(Dr. Clark’s statements as to his background and qualifications, definition of
`the person of ordinary skill in the art, and background on the relevant
`technology). At this stage of the proceeding, Patent Owner has not
`submitted, nor was it required to submit, similar testimony evidence.
`LARSEN
`E.
`Larsen is the August 13, 2015, published version of U.S. Application
`14/405,072, filed on June 7, 2013. Ex. 1003, codes (43), (21), (22).4
`Larsen’s Abstract states: “The present invention relates to polypeptides,
`specifically polypeptides having transgalactosylating activity and nucleic
`acids encoding these, and their uses in e.g. dairy product.” Ex. 1003,
`Abstract; see also id. ¶ 1.
`As background, Larsen explains that
`Galactooligosaccharides (GOS) are carbohydrates which
`are nondigestable in humans and animals comprising two or
`more galactose molecules, typically up to nine, linked by
`glycosidic bonds. GOS’s [sic] may also include one or more
`glucose molecules. One of the beneficial effects of GOS’s [sic]
`is their ability of acting as prebiotic compounds by selectively
`stimulating the proliferation of beneficial colonic
`microorganisms such as bacteria to give physiological benefits
`to the consumer. The established health effects have resulted in
`
`
`4 Larsen ultimately issued on January 14, 2020, as U.S. Patent 10,531,672
`B2. Ex. 2001, 1 (issue notification).
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`Patent 10,058,107 B2
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`
`a growing interest in GOSs as food ingredients for various
`types of food.
`Id. ¶ 2. Larsen discloses that “[t]he enzyme β-galactosidase (EC 3.2.1.23)
`usually hydrolyses lactose to the monosaccharides D-glucose and D-
`galactose,” but “some β-galactosidases are able to transfer galactose to the
`hydroxyl groups of D-galactose or D-glucose in a process called
`transgalactosylation whereby galacto-oligosaccharides are produced.” Id.
`¶ 3.
`
`Larsen discloses that “[i]t is an object of embodiments of the
`invention to provide a polypeptide which has a useful ratio of
`transgalactosylation to hydrolysis activity and thus [is an] efficient
`producer[ ] of GOS when incubated with lactose even at low lactose levels
`such as in a milk-based product.” Id. ¶ 10. Larsen states that
`“‘Transgalactosylase’ means an enzyme that, among other things, is able to
`transfer galactose to the hydroxyl groups of D-galactose or D-glucose
`whereby galacto-oligosaccharides are produced,” and discloses
`enzymes/polypeptides having this β-galactosidase, transgalactosylation
`activity. Id. ¶ 67. Larsen states that its “invention also encompasses
`variants, homologues and derivatives of any amino acid sequence of a
`protein or polypeptide as defined herein, particularly those of SEQ ID NO: 1
`. . . .” Id. ¶ 197. Larsen discloses that “SEQ ID NO: 1 (also named
`(BIF_917) herein) is a 887 amino acid truncated fragment of SEQ ID NO:
`22.” Id. ¶ 42; see also id. at 30 (SEQ ID NO: 1 (BIF_917)).
`Larsen discloses that
`The present invention encompasses polypeptides having
`a certain degree of sequence identity or sequence homology
`with amino acid sequence(s) defined herein or with a
`polypeptide having the specific properties defined herein. The
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`Patent 10,058,107 B2
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`
`present invention encompasses, in particular, peptides having a
`degree of sequence identity with any one of SEQ ID NO: 1, 2,
`3, 4 or 5, defined below, or homologues thereof. . . .
`The sequences, particularly those of variants,
`homologues and derivatives of SEQ ID NO: 1, 2, 3, 4 or 5
`defined below, may also have deletions, insertions or
`substitutions of amino acid residues which produce a silent
`change and result in a functionally equivalent substance.
`Deliberate amino acid substitutions may be made on the basis
`of similarity in polarity, charge, solubility, hydrophobicity,
`hydrophilicity, and/or the amphipathic nature of the residues as
`long as the secondary binding activity of the substance is
`retained. For example, negatively charged amino acids include
`aspartic acid and glutamic acid; positively charged amino acids
`include lysine and arginine; and amino acids with uncharged
`polar head groups having similar hydrophilicity values include
`leucine, isoleucine, valine, glycine, alanine, asparagine,
`glutamine, serine, threonine, phenylalanine, and tyrosine.
`The present invention also encompasses conservative
`substitution (substitution and replacement are both used herein
`to mean the interchange of an existing amino acid residue, with
`an alternative residue) that may occur i.e. like-for-like
`substitution such as basic for basic, acidic for acidic, polar for
`polar etc. Non-conservative substitution may also occur i.e.
`from one class of residue to another or alternatively involving
`the inclusion of unnatural amino acids such as ornithine
`(hereinafter referred to as Z), diaminobutyric acid ornithine
`(hereinafter referred to as B), norleucine ornithine (hereinafter
`referred to as O), pyriylalanine, thienylalanine, naphthylalanine
`and phenylglycine.
`Conservative substitutions that may be made are, for
`example within the groups of basic amino acids (Arginine,
`Lysine and Histidine), acidic amino acids (glutamic acid and
`aspartic acid), aliphatic amino acids (Alanine, Valine, Leucine,
`Isoleucine), polar amino acids (Glutamine, Asparagine, Serine,
`Threonine), aromatic amino acids (Phenylalanine, Tryptophan
`and Tyrosine), hydroxyl amino acids (Serine, Threonine), large
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`
`amino acids (Phenylalanine and Tryptophan) and small amino
`acids (Glycine, Alanine).
`In one aspect, the polypeptide sequence used in the
`present invention is in a purified form. In one aspect, the
`polypeptide or protein for use in the present invention is in an
`isolated form.
`In one aspect, the polypeptide of the present invention is
`recombinantly produced.
`The variant polypeptides include a polypeptide having a
`certain percent, e.g., at least 90%, 91%, 92%, 93%, 94%, 95%,
`96%, 97%, 98%, or 99%, of sequence identity with SEQ ID
`NO: 1 or 2.
`Id. ¶¶ 194, 198–203; see also id. at claim 1 (claiming a polypeptide having
`transgalactosylation activity comprising an amino acid sequence having at
`least 90% sequence identity with SEQ ID NO: 1). Regarding such changes
`to its SEQ ID NO: 1 polypeptide (“BIF917”), Larsen teaches that a
`substitution or deletion of 1–10 amino acids can occur in the N-terminal end
`of the polypeptide. Id. ¶ 219.
`Larsen discloses examples of the BIF917 polypeptide, and indicates
`that it exhibits β-galactosidase activity. Id. ¶¶ 469–471, 479–504. Larsen
`discloses that BIF917 and one other tested variant had the highest ratio of
`transgalactosylation activity, around 250%. Id. ¶¶ 471, 474, 504.
`II. DISCUSSION
`LEVEL OF ORDINARY SKILL IN THE ART
`Petitioner states,
`a person of ordinary skill in the art at all relevant times would
`have had a Ph.D. or master’s degree in chemistry, chemical
`engineering, biochemical engineering, molecular biology, or a
`related technical field, with several years of experience
`studying, developing, or using enzymes such as
`β-galactosidases in industrial processes.
`
`A.
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`Patent 10,058,107 B2
`
`Pet. 31–32 (citing Ex. 1002 ¶ 43 (Clark Declaration)); see also id. at 58–59
`(reiterating this definition and indicating “[t]he level of ordinary skill was
`high and the field was advanced by Novozyme’s earliest possible effective
`filing date in 2017”).
`Patent Owner states it “does not agree that Petitioner’s definition of a
`POSA is correct. Regardless, even under Petitioner’s definition, Petitioner’s
`obviousness challenge fails.”5 Prelim. Resp. 22, n.7. Other than expressing
`its disagreement, Patent Owner neither directly challenges Petitioner’s
`definition nor offers its own definition. See generally id.
`For purposes of this Decision, at this stage of the proceeding, we
`accept Petitioner’s proposed definition of the person of ordinary skill in the
`art, or skilled artisan, which is not substantively opposed by Patent Owner
`and appears to be consistent with the level of skill in the art reflected in the
`prior art of record and the disclosure of the ’107 patent. See Okajima v.
`Bourdeau, 261 F.3d 1350, 1355 (Fed. Cir. 2001) (“the prior art itself [may]
`reflect[] an appropriate level” as evidence of the level of ordinary skill in the
`art) (quoting Litton Indus. Prods., Inc. v. Solid State Sys. Corp., 755 F.2d
`158, 163 (Fed. Cir. 1985)).
`CLAIM CONSTRUCTION
`B.
`The Board interprets claim terms in an inter partes review using the
`same claim construction standard that is used to construe claims in a civil
`action in federal district court. 37 C.F.R. § 42.100(b) (2020). In construing
`claims, district courts and the Board here, by default, give claim terms their
`ordinary and customary meaning, which is “the meaning that the term would
`
`
`5 Petitioner uses the acronym POSA to refer to the person of ordinary skill in
`the art.
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`have to a person of ordinary skill in the art in question at the time of the
`invention.” Phillips v. AWH Corp., 415 F.3d 1303, 1312–13 (Fed. Cir.
`2005) (en banc).
`Should claim terms require express construction, sources for claim
`interpretation include “the words of the claims themselves, the remainder of
`the specification, the prosecution history [i.e., the intrinsic evidence], and
`extrinsic evidence concerning relevant scientific principles, the meaning of
`technical terms, and the state of the art.” Id. at 1314 (quoting Innova/Pure
`Water, Inc. v. Safari Water Filtration Sys., Inc., 381 F.3d 1111, 1116 (Fed.
`Cir. 2004)). “[T]he claims themselves [may] provide substantial guidance as
`to the meaning of particular claim terms.” Id. However, the claims “do not
`stand alone,” but are part of “‘a fully integrated written instrument,’
`consisting principally of a specification that concludes with the claims,” and,
`therefore, the claims are “read in view of the specification.” Id. at 1315
`(quoting Markman v. Westview Instruments, Inc., 52 F.3d 967, 978–79 (Fed.
`Cir. 1995) (en banc)).
`Any special definition for a claim term must be set forth in the
`specification with reasonable clarity, deliberateness, and precision. In re
`Paulsen, 30 F.3d 1475, 1480 (Fed. Cir. 1994). Without such a special
`definition, however, limitations may not be read from the specification into
`the claims. In re Van Geuns, 988 F.2d 1181, 1184 (Fed. Cir. 1993).
`“[W]e need only construe terms ‘that are in controversy, and only to
`the extent necessary to resolve the controversy . . . .’” Nidec Motor Corp. v.
`Zhongshan Broad Ocean Motor Co., 868 F.3d 1013, 1017 (Fed. Cir. 2017)
`(quoting Vivid Techs., Inc. v. Am. Sci. & Eng’g, Inc., 200 F.3d 795, 803
`(Fed. Cir. 1999)).
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`
`Petitioner proposes that the claim language “transgalactosylating
`activity” should be interpreted “[c]onsistent with the ordinary meaning of
`this term to persons skilled in the art, . . . [which] refer[s] to the transfer of a
`galactose moiety to a molecule other than water to produce
`galactooligosaccharides.” Pet. 32 (citing, inter alia, Ex. 1001, 2:8–14, 2:32–
`43; Ex. 1002 ¶ 44). Petitioner asserts “[t]his common understanding of
`transgalactosylating activity is consistent with the ’107 patent specification,
`which states that transgalactosylation produces galactooligosaccharides,
`resulting in lower galactose concentrations compared to glucose” and that
`“the plain language of the claims imposes no limitation on the amount or
`degree of transgalactosylating activity.” Id. at 32–33 (citing Ex. 1001,
`16:40–18:23, 23:40–24:46; Ex. 1002 ¶ 45). Petitioner asserts that:
`Thus, the Board should also construe
`“transgalactosylating activity” in the challenged claims to have
`no limitation on the ratio of transgalactosylating activity to
`lactase (hydrolyzing) activity, broadly encompassing
`polypeptides and fragments that are primarily
`transgalactosylating in their activity, including polypeptides
`that have high ratios of transgalactosylating to lactase
`(hydrolyzing) activity.
`Id. at 33.
`Patent Owner responds:
`Petitioner proposes a construction of
`“transgalactosylating activity,” arguing that the plain language
`of the claims imposes no limitation on the amount or degree of
`transgalactosylating activity. Petition at 32. Thus, under
`Petitioner’s construction, “transgalactosylating activity” does
`not require any particular amount or ratio of
`transgalactosylating activity.
`Patent Owner does not concede that Petitioner’s proposed
`constructions are correct. Nevertheless, even under Petitioner’s
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`proposed construction, Petitioner fails to demonstrate a
`reasonable likelihood that any of the challenged claims are
`unpatentable.
`Prelim. Resp. 7. Patent Owner does not offer any proposed definition for
`this claim term.
`We decline to expressly adopt a proposed construction of the claim
`language at this time, but instead, based on the information presented, the
`claim language carries its ordinary meaning as it would have been
`understood by a person of ordinary skill in the art, which appears to be the
`result argued for by each party. Vivid Techs., 200 F.3d at 803 (“[O]nly those
`terms need be construed that are in controversy, and only to the extent
`necessary to resolve the controversy.”).
`The claim language “transgalactosylating activity” is understandable
`on its face as a well-understood term of art; neither party argues otherwise.
`See generally, e.g., Ex. 1001; Ex. 1003; Ex. 1004; Ex. 1005; Ex. 1006. The
`evidence of record does not indicate that this term has any special meaning
`different than what the plain language in context would suggest. The ’107
`patent does not expressly assign a special meaning to the language
`“transgalactosylating activity.” See generally Ex. 1001. We find that the
`record at this stage supports that the person of ordinary skill in the art would
`have understood this term, and that it needs no special interpretation at this
`point in the proceeding.6
`
`
`6 Because our institution decision does not turn on whether one of ordinary
`skill would understand that the claims are limited to polypeptides having
`primarily transgalactosylating activity, we decline to address here that
`portion of Petitioner’s proposed construction.
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`C. APPLICABLE LEGAL STANDARDS
`“In an IPR, the petitioner has the burden from the onset to show with
`particularity why the patent it challenges is unpatentable.” Harmonic Inc. v.
`Avid Tech., Inc., 815 F.3d 1356, 1363 (Fed. Cir. 2016) (citing 35 U.S.C.
`§ 312(a)(3) (requiring inter partes review petitions to identify “with
`particularity . . . the evidence that supports the grounds for the challenge to
`each claim”)). This burden of persuasion never shifts to Patent Owner. See
`Dynamic Drinkware, LLC v. Nat’l Graphics, Inc., 800 F.3d 1375, 1378
`(Fed. Cir. 2015) (discussing the burden of proof in inter partes review).
`Regarding a patent’s assertion of priority for its claims to a date
`earlier than its actual filing date, “[i]n order to gain the benefit of the filing
`date of an earlier application under 35 U.S.C. § 120, each application in the
`chain leading back to the earlier application must comply with the written
`description requirement of 35 U.S.C. § 112.” Lockwood v. American
`Airlines, Inc., 107 F.3d 1565, 1571 (Fed. Cir. 1997); see also 35 U.S.C.
`§ 120 (“An application for patent for an invention disclosed in the manner
`provided by section 112(a) (other than the requirement to disclose the best
`mode) in an application previously filed in the United States, or as provided
`by section 363 . . . shall have the same effect, as to such invention, as though
`filed on the date of the prior application . . . .”). Thus, a claim for priority to
`earlier-filed applications depends on those applications’ compliance with
`Section 112 (enablement and written description) in view of the newly filed
`claims.
`“In order to satisfy the written description requirement, the disclosure
`as originally filed does not have to provide in haec verba support for the
`claimed subject matter at issue,” but the disclosure must convey with
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`reasonable clarity to those skilled in the art that the inventor was in
`possession of the invention. Purdue Pharma L.P. v. Faulding, Inc., 230
`F.3d 1320, 1323 (Fed. Cir. 2000). “The purpose of the written description
`requirement is to prevent an applicant from later asserting that he invented
`that which he did not.” Amgen, Inc. v. Hoechst Marion Roussel, Inc., 314
`F.3d 1313, 1330 (Fed. Cir. 2003). “Entitlement to a filing date does not
`extend to subject matter which is not disclosed, but would be obvious over
`what is expressly disclosed. It extends only to that which is disclosed.”
`Lockwood, 107 F.3d at 1571–72.
`The level of disclosure required to provide a sufficient written
`description under Section 112 depends on the subject matter and breadth
`claimed, for example, whether a claim covers a species or a genus and
`whether a claim relies on recited functionality, rather than structure, as a
`limitation. A “disclosure that names one species encompassed within a
`genus will adequately describe a claim directed to that genus only if the
`disclosure ‘indicates that the patentee has invented species sufficient to
`constitute the gen[us]’” and “a patentee will not be deemed to have invented
`species sufficient to constitute the genus by virtue of having disclosed a
`single species when . . . the evidence indicates ordinary artisans could not
`predict the operability in the invention of any species other than the one
`disclosed.” In re Curtis, 354 F.3d 1347, 1358 (Fed. Cir. 2004). For
`example, “[a] description of a genus of cDNAs may be achieved by means
`of a recitation of a representative number of cDNAs, defined by nucleotide
`sequence, falling within the scope of the genus or of a recitation of structural
`features common to the members of the genus, which features constitute a
`substantial portion of the genus,” but if a specification “does not define any
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`structural features commonly possessed by members of the genus that
`distinguish [its species] from others[,] [o]ne skilled in the art . . . cannot, as
`one can do with a fully described genus, visualize or recognize the identity
`of the members of the genus.” Regents of the Univ. of California v. Eli Lilly
`and Co., 119 F.3d 1559, 1568–69 (Fed. Cir. 1997).
`Moreover, the converse is true in that “one cannot disclose a forest in
`the original application, and then later pick a tree out of the forest and say
`‘here is my invention.’ In order to satisfy the written description
`requirement, the blaze marks directing the skilled artisan to that tree must be
`in the originally filed disclosure.” Purdue Pharma L.P. v. Faulding, Inc.,
`230 F.3d 1320, 1326–27 (Fed. Cir. 2000).
`Regarding obviousness, the Supreme Court in KSR International Co.
`v. Teleflex Inc., 550 U.S. 398 (2007), reaffirmed the framework for
`determining obviousness set forth in Graham v. John Deere Co., 383 U.S. 1
`(1966). The KSR Court summarized the four factual inquiries set forth in
`Graham (383 U.S. at 17–18) that are applied in determining whether a claim
`is unpatentable as obvious under 35 U.S.C. § 103 as follows:
`(1) determining the scope and content of the prior art; (2) ascertaining the
`differences between the prior art and the claims at issue; (3) resolving the
`level of ordinary skill in the art;7 and (4) considering objective evidence
`indicating obviousness or non-obviousness.8 KSR, 550 U.S. at 406.
`
`
`7 At this stage of the proceeding, there is no dispute as to the level of
`ordinary skill in the art. See supra Section II.A.
`8 At this stage of the proceeding, there is no evidence pertaining to objective
`indicia of non-o