DSM IP Assets, B.V. et al v. Lallemand Specialties, Inc. et al

Filing 151

PROPOSED CLAIM CONSTRUCTIONS. Signed by District Judge William M. Conley on 3/7/2018. (arw)

IN THE UNITED STATES DISTRICT COURT
FOR THE WESTERN DISTRICT OF WISCONSIN
DSM IP ASSETS, B.V. & DSM BIO-BASED
PRODUCTS & SERVICES, B.V.,
Plaintiffs and Counter-Defendants,
v.

PROPOSED CLAIMS
CONSTRUCTIONS
16-cv-497-wmc

LALLEMAND SPECIALTIES, INC. &
MASCOMA LLC,
Defendants and Counterclaimants.

Plaintiffs DSM IP Assets, B.V. and DSM Bio-Based Products & Services B.V.
(collectively “DSM”) bring this patent infringement action against Lallemand Specialties,
Inc. and Mascoma LLC (collectively “Lallemand”) concerning U.S. Patent No. 8,795,998
(the “’998 patent”). Specifically, DSM alleges that Lallemand’s products, TransFerm
Yield+ (“TFY+”) and YP3, infringe.

The purpose of this opinion is to provide the

parties with the court’s proposed claim constructions and the reasoning behind them in
advance of the scheduled expert colloquy on Friday, March 16, 2018.

OPINION
“‘[T]he claims of a patent define the invention to which the patentee is entitled
the right to exclude.’” Phillips v. v. AWH Corp., 415 F.3d 1303, 1312 (Fed. Cir. 2005)
(en banc) (quoting Innova/Pure Water, Inc. v. Safari Water Filtration Sys., Inc., 381 F.3d
1111, 1115 (Fed. Cir. 2004)). For this reason, the right to exclude “begins and ends . . .
with the actual words of the claim.” Renishaw PLC v. Marposs Societa’ Per Azioni, 158 F.3d
1243, 1248 (Fed. Cir. 1998). The goal of claims construction “is to give claim terms the

meaning understood by a person of ordinary skill in the art at the time of invention.”
Mass. Inst. of Tech. v. Shire Pharms., Inc., 839 F.3d 1111, 1118 (Fed. Cir. 2016)
[hereinafter MIT] (citing Phillips, 415 F.3d at 1312-14). While this includes “a heavy
presumption that claim terms are to be given their ordinary and customary meaning,” id.
at 1118 (quoting Aventis Pharm. Inc. v. Amino Chems. Ltd., 715 F.3d 1363, 1373 (Fed. Cir.
2013)), this “meaning” is what a person of ordinary skill in the art would have after
reading the entire patent, id. (quoting Phillips, 415 F.3d at 1321). See also Renishaw, 158
F.3d at 1250 (“Ultimately, the interpretation to be given a term can only be determined
and confirmed with a full understanding of what the inventors actually invented and
intended to envelop with the claim.” (citing Markman v. Westview Instruments, Inc., 517
U.S. 370, 389 (1996))).
For patent claims in highly specialized fields of study, like that at issue here,
“determining the ordinary and customary meaning of the claim requires examination of
terms that have a particular meaning in a field of art,” yet are “not immediately
apparent,” requiring the court to examine intrinsic and extrinsic evidence “‘concerning
the relevant scientific principles, the meaning of technical terms, and the state of the
art.’” Phillips, 415 F.3d at 1314 (quoting Innova, 381 F.3d at 1116).1 Similarly, while
the “ordinary meaning” inquiry remains “an objective baseline from which to begin claim
interpretation,” id. at 1313 (citing Innova, 381 F.3d at 1116), where a patent fails to
explicitly define a disputed or arguably ambiguous term, the court may look to the patent

1

Intrinsic evidence includes the patent itself and the file history, while extrinsic evidence includes
evidence like expert testimony, dictionaries, inventor testimony, technical treatises and articles, or
evidence of prior art. See Vitronics Corp. v. Conceptronic, Inc., 90 F.3d 1576, 1584 (Fed. Cir. 1996).

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as a whole, including its prosecution history, to determine that term’s meaning, Wi-LAN
USA, Inc. v. Apple Inc., 830 F.3d 1374, 1387 (Fed. Cir. 2016) (citing Phillips, 415 F.3d at
1315). See also Renishaw, 158 F.3d at 1248 (“The intrinsic evidence, and, in some cases,
the extrinsic evidence, can shed light on the meaning of the terms recited in a claim,
either by confirming the ordinary meaning of the claim terms or by providing special
meaning for claim terms.” (citing Vitronics, 90 F.3d at 1583)). Still, claims construction
is viewed as a question of law, Wi-LAN, 830 F.3d at 1381, reserved only for the court,
Teva Pharms. USA, Inc. v. Sandoz, Inc., 135 S.Ct. 831, 835 (2015).
Here, the parties dispute the proper construction of four terms, all found in claim
1. (See Joint Statement on Claims Construction (dkt. #44) 2-3; ’998 Patent (dkt. #1-1)
40 (67:12-37).) Plaintiffs claim that all four of their proposed constructions are faithful
to the terms’ “[p]lain and ordinary meaning[s],” although even they put a gloss on
certain terms, while defendants claim that some terms require further construction to be
consistent with the claimed invention and prosecution history.

(Joint Statement on

Claims Construction (dkt. #44) 2-3.) With emphasis on the terms in dispute, Claim 1
specifies:
1. Transgenic yeast cells comprising one or more recombinant
heterologous, nucleic acid sequences encoding a protein with
NAD+-dependent acetylating acetaldehyde dehydrogenase
activity (EC 1.2.1.10),
wherein said cells lack enzymatic activity needed for the
NADH-dependent glycerol synthesis, or
said cells have a reduced enzymatic activity with respect to
the NADH-dependent glycerol synthesis
compared to a corresponding wild-type yeast cell, and
wherein said cells are free of NAD-dependent glycerol 3phosphate dehydrogenase activity or have reduced NADdependent glycerol 3-phosphate dehydrogenase activity

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compared to corresponding wild-type cells, and/or
wherein the cells are either free of glycerol phosphate
phosphatase activity or have reduced glycerol phosphate
phosphatase activity compared to corresponding wild-type
cells, and
which comprise a genomic mutation in at least one gene
selected from the group consisting of GPD2, GPD2, GPP1
and GPP2, and
wherein said cells further comprise one or more nucleic acid
sequences encoding an acetyl-Coenzyme A synthetase activity
(EC 6.2.1.1) and one or more nucleic acid sequences
encoding NAD+-dependent alcohol dehydrogenase activity
(EC 1.1.1.1).
(’998 Patent (dkt. 1-1) 40 (67:12-37) (emphasis added).) The court addresses each of
the four disputed terms below.
Term 1
“one or more recombinant heterologous, nucleic acid sequences encoding a protein with
NAD+-dependent acetylating acetaldehyde dehydrogenase activity (EC 1.2.1.10)”
DSM’s Proposed Construction

Lallemand’s Proposed Construction

“one or more recombinant heterologous, “a recombinant heterologous, nucleic acid
nucleic acid sequences that encode a encoding an NAD+-dependent acetylating
protein
having
NAD+-dependent acetaldehyde dehydrogenase enzyme”
acetylating acetaldehyde dehydrogenase
activity (EC 1.2.1.10)”

DSM proposes changing “nucleic acid sequences encoding a protein with NAD+dependent acetylating acetaldehyde dehydrogenase activity” to “nucleic acid sequences
that encode a protein having NAD+-dependent acetylating acetaldehyde dehydrogenase
activity.”

In contrast, Lallemand proposes: (a) limiting the cells to having a

“recombinant heterologous, nucleic acid” instead of the possibility of one or more
“recombinant heterologous[] nucleic acid sequences” and (b) encompassing an “NAD+dependent acetylating acetaldehyde dehydrogenase enzyme” instead of “a protein with
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NAD+-dependent acetylating acetaldehyde dehydrogenase activity (EC 1.2.1.10).”
Plaintiffs explain that EC numbers classify enzymes based on the reaction they
catalyze, which means the “EC 1.2.1.10” is reserved for proteins that catalyze the
conversion of acetyl-Coenzyme A to acetaldehyde. (Pls.’ Opening Br. (dkt. #59) 15.) In
response, defendants argue that the claim specifies a protein that has “NAD+-dependent
acetylating acetaldehyde dehydrogenase activity” -- a particular enzymatic activity.
(Defs.’ Opp’n (dkt. #77) 26-27.)

Plaintiffs characterize this dispute as a question

whether AdhE and other bifunctional acetylating acetaldehyde dehydrogenase enzymes
are included, adding that because the patent identifies AdhE it would be improper to
exclude a preferred embodiment. (Pls.’ Reply (dkt. #97) 8-9.)
The court will not adopt either side’s proposed construction, having determined
that the plain and ordinary meaning of this term is indeed appropriate. As an initial
matter, the court sees no reason to limit the term to a single “recombinant heterologous[]
nucleic acid,” where the term specifies “one or more . . . sequences.” As to plaintiffs’
proposal to change the word “encoding” to “that encode,” the court is unconvinced that
there is a meaningful difference, as importantly, if there is a difference, no basis to depart
from the claim’s actual syntax exists. The court also rejects defendants’ proposed change
of “NAD+-dependent acetylating acetaldehyde dehydrogenase activity (EC 1.2.1.10)” to
“NAD+-dependent acetylating acetaldehyde dehydrogenase enzyme.” As plaintiffs point
out, the Enzyme Commission number -- the EC number -- is a unique four-digit number
which describes the chemical reaction catalyzed. Specifically, the first digit identifies one
of six classes; “the second and third digits describe the type of reaction catalyzed”; and

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“the fourth digit is employed to distinguish between enzymes of the same function on the
basis of the actual substrate in the reaction catalyzed.” Douglas S. Clark & Harvey W.
Blanch, Biochemical Engineering 1 (2d. ed. 1997). The enzyme identified by “EC 1.2.1.10”
is “acetaldehyde dehydrogenase (acetylating).”

Information on EC 1.2.1.10 --

acetaldehyde

BRENDA,

dehydrogenase

(acetylating),

https://www.brenda-

enzymes.org/enzyme.php?ecno=1.2.1.10 (last visited Mar. 1, 2018).

Replacing

“activity” with “enzyme” would appear to change the claim’s meaning since it is the
activity -- not the enzyme that performs the activity -- that is at the heart of this portion
of the claim term and, indeed, the invention itself. Thus, this term simply means “one or
more recombinant heterologous, nucleic acid sequences encoding a protein with NAD+dependent acetylating acetaldehyde dehydrogenase activity (EC 1.2.1.10).”

(See ’998

Patent (dkt. 1-1) 40 (67:12-15).)
The parties discuss the second and third terms together, and the court will follow
suit, while actually construing the terms in dispute individually.
Term 2
“said cells . . . have reduced NAD-dependent glycerol 3-phosphate dehydrogenase
activity [GPD] compared to corresponding wild-type cells”
DSM’s Proposed Construction

Lallemand’s Proposed Construction

“the cells exhibit a reduction in the rate of
the reaction catalyzed by GPD in the
enzymatic
production
of
glycerol
compared to the corresponding wild-type
yeast cells”

“the cells include modifications to one or
more genes encoding GPD activity such
that GPD is expressed considerably less
than in the wild-type yeast cell or such
that one or more genes encode GPD with
reduced activity”

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Term 3
“said cells have a reduced enzymatic activity with respect to the NADH-dependent
glycerol synthesis compared to corresponding wild-type cells”
DSM’s Proposed Construction

Lallemand’s Proposed Construction

“the cells exhibit a reduction in the rate of “the cells include modifications to one or
enzymatic production of glycerol compared more genes encoding one or more enzymes
needed for NADH-dependent glycerol
to the corresponding wild-type yeast cell”
synthesis such that one or more enzymes
are expressed considerably less than in the
wild-type yeast cell or such that one or
more genes encode a polypeptide with
reduced activity”

DSM argues that “enzymatic activity” is defined by enzymology and metabolic
engineering as “the enzyme-catalyzed rate of product conversion under a given set of
conditions, usually measured as the concentration change (substrate consumption or
product formation) per unit time,” which is usually expressed “in terms of units based
upon the rate of the reaction that the enzyme promotes.” (Pls.’ Opening Br. (dkt. #59)
18.) According to DSM, therefore, “‘enzymatic activity’ is synonymous with the rate of
the enzyme-catalyzed reaction, with an increased enzymatic activity corresponding to an
increased reaction rate (due to lower activation energy) and a reduced enzymatic activity
corresponding to a reduced reaction rate (due to a higher activation energy).” (Id. at 19.)
Thus, DSM argues that both “reduced enzymatic activity terms” should be construed to
mean: “(1) the cells exhibit a reduction in the rate of enzymatic production of glycerol
compared to corresponding wild-type yeast cells; and (2) the cells exhibit a reduction in
the rate of the reaction catalyzed by GPD in the enzymatic production of glycerol

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compared to the corresponding wild-type yeast cells.” (Id.)
Lallemand counters that DSM’s proposed constructions would render any
reduction in glycerol production an infringement, but that unreasonably and
unnecessarily simplifies the claims. Lallemand further argues that DSM’s reading must
be rejected for three additional reasons: (1) inappropriately including “enzymatic
production of glycerol” in both terms would make one superfluous; (2) intrinsic evidence
establishes that “enzymatic activity” refers to the amount of enzyme expressed making it
improper to equate enzymatic activity with the rate of substrate consumption or product
formation; and (3) no extrinsic evidence requires a different meaning for “enzymatic
activity.” (Defs.’ Opp’n (dkt. #77) 7-8.) In response, DSM first points out that its
construction does not make one term superfluous because a reduction in enzymatic
activity could be achieved under Claim 1 by deleting GPP activity -- without necessarily
impacting the GPD-catalyzed reaction at all. (Pls.’ Reply (dkt. #97) 12.) Secondly,
DSM explains that enzymatic activity cannot mean the “amount of enzyme” because
enzymatic activity is dependent on other factors, such as temperature, pH, and substrate
concentration. (Id. at 26.) Further, DSM argues, the structural requirement of genetic
modification comes from a different term, and it need not, and should not, be read into
terms 2 and 3, especially because the specification contemplates other methods. (Id. at
13-14; Pls.’ Opening Br. (dkt. #59) 19-20.)

Third, DSM argues that Lallemand’s

proposed construction would actually exclude the embodiment introducing a separate
metabolic pathway to compete with the NADH-glycerol synthesis pathway. (Pls.’ Reply
(dkt. #97) 15-16.)

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Finally, Lallemand likewise emphasizes that its proposed constructions of terms 2
and 3 differ from DSM’s in two ways: (1) the meaning of “enzymatic activity”; and (2)
the structural requirements necessary for a “reduction.” (Defs.’ Opening Br. (dkt. #64)
15.) As to the meaning of “enzymatic activity,” Lallemand proposes construing it as a
measure of the expression or availability of GPD in the cell, while DSM construes it as a
measurement of the rate of the GPD-catalyzed reaction.

As to the structural

requirements necessary to measure “a reduction,” Lallemand proposes tying the reduction
to the genetic modification, while DSM does not.
As an initial matter, “activity” is a noun that refers here to a metabolic process,
whose “rate” would normally be understood by one skilled in the art to be measured by
the change in moles of a substrate converted or of its converted product per unit of time.
Here, GPD [an enzyme] catalyzes the conversion of dihydroxyacetone phosphate
(“DHAP”) to glycerol-3-phosphate (“G-3-P”), so that “activity” is measured by the
change in DHAP or the change in G-3-P over time.2
Turning to term 2, the plain language simply provides that the patented cells have
reduced GPD activity as compared to wild-type cells. Contrary to Lallemand’s proposal,
this language does not limit the reduction in the rate of activity to a genetic modification
removing or reducing production of GPD; indeed, term 2 does not specify the means by

2

The conversion of DHAP to G-3-P generally involves a 1:1 reaction ratio so the rate of change in
either the concentration of DHAP or the concentration of G-3-P divided by the amount of time
should provide an approximately equal measure of activity. This reaction can be displayed as:
G-3-P
DHAP

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which the reduction is achieved.3
Accordingly, DSM’s proposal specifying that the cells “exhibit a reduction in the
rate of the reaction catalyzed by GPD” is a clarification of the “have reduced NADdependent glycerol 3-phosphate dehydrogenase activity [GPD]” language found in the
term. Similarly, DSM’s addition of “enzymatic production of glycerol” further clarifies
that the claim term is talking about GPD’s function in the production of glycerol, not its
other possible functions. As such, the court will adopt DSM’s proposal as to term 2,
construing it as “said cells exhibit a reduction in the rate of the reaction catalyzed by
GPD in the enzymatic production of glycerol compared to the corresponding wild-type
yeast cells.”
For similar reasons, DSM’s proposed construction of term 3 is closer to the mark
than Lallemand’s proposal.

Term 3 specifies that the patented cells have decreased

metabolic activity regarding the NADH-dependent glycerol synthesis as compared to
wild-type cells.

As with term 2, term 3 does not require genetic modification.4

Accordingly, DSM’s proposed language -- “exhibit a reduction in the rate” -- provides
appropriate clarification. However, the term’s construction should maintain a specific

3

In fact, genetic modification is required by a different term. (’998 Patent (dkt. #1-1) at 40
(67:30-32 (“which comprise a genomic mutation in at least one gene selected from the group
consisting of GPD1, GPD2, GPP1, and GPP2”)); id. (68:39-41 (“The cells of claim 1, wherein at
least one said mutation is a complete deletion of said gene in comparison to the corresponding
wild-type yeast gene.”)).) Reading the genetic modification requirement into this term would
make the later term superfluous. See WiLAN, 830 F.3d at 1391 (noting the “presumption
that differently worded claims cover different claim scope,” stemming from “the legal canon
of construction against superfluity” such that “[a] construction that would cause two
differently worded claims to cover exactly the same claim scope would render one of the
claims superfluous, so [courts] apply a presumption against such constructions”).

4

See supra, note 3.

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reference to the “NADH-dependent glycerol synthesis.” Thus, term 3 will be construed
to mean “said cells exhibit a reduction in the rate of NADH-dependent glycerol
production compared to the corresponding wild-type yeast cell.”
Term 4
“wherein said cells further comprise one or more nucleic acid sequences encoding an
acetyl-Coenzyme A synthetase activity (EC 6.2.1.1) and one or more nucleic acid
sequences encoding NAD+-dependent alcohol dehydrogenase activity (EC 1.1.1.1)”
DSM’s Proposed Construction

Lallemand’s Proposed Construction

“the cells comprise (i) one or more nucleic
acid sequences that encode an acetylCoenzyme A synthetase activity and
(ii) one or more nucleic acid sequences that
encode
an
NAD+-dependent
dehydrogenase activity”

“wherein said cells further comprise one or
more nucleic acid sequences encoding an
acetyl-Coenzyme A synthetase activity and
one or more nucleic acid sequences
encoding
NAD+-dependent
alcohol
dehydrogenase activity, whereby the cells
are net consumers of acetate/acetic acid
such that the cells can reoxidize NADH by
the reduction of acetate/acetic acid to
ethanol via NADH-dependent reactions in
place of glycerol synthesis and whereby the
cells grow preferentially in the presence of
acetate”

The parties basically agree on the substance of DSM’s proposed construction.5
The dispute arises from Lallemand’s three additional limitations: (1) “the cells are net
consumers of acetate/acetic acid”; (2) “the cells can reoxidize NADH by the reduction of
acetate/acetic acid to ethanol via NADH-dependent reactions in place of glycerol
synthesis”; and (3) “the cells grow preferentially in the presence of acetate.” Lallemand
5

There are two slight differences: (1) DSM modifies “encoding” to “that encode,” while
Lallemand uses “encoding” as found in the disputed term; and (2) DSM removes the “alcohol”
from the “NAD+-dependent alcohol dehydrogenase activity,” while Lallemand keeps it in,
consistent with the disputed term. (The addition of the romanettes in DSM’s proposal is nonsubstantive, while improving readability.)

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argues that its additions are based on the patent applicant’s statements to distinguish the
invention from the prior art.

(Defs.’ Opp’n (dkt. #77) 18.) Specifically, Lallemand

bases the first addition on the patent applicant’s statement that “[t]here is no suggestion
to modify a yeast cell in order to make it a net consumer of acetate”; the second addition
is based on a statement that the invention “is capable of using acetate as an electron
acceptor to reoxidize NADH and therefore avoids or reduces the need for glycerol
synthesis”; and the third addition on “[t]he invention provides a yeast cell that actually
grows preferentially in the presence of acetate.” (Id. at 24.)
DSM argues that Lallemand has failed to meet the “high standard” of establishing
prosecution disclaimer. (Pls.’ Opening Br. (dkt. #59) 24-25 (citing MIT, 839 F.3d at
1119).) As to the first two additions, in particular, DSM argues that the ability of the
cells to use the acetate in the production of ethanol instead of glycerol is a “further
advantage,” not a disclaimer. (Id. at 25-26.) Further, DSM argues that “Lallemand’s
argument is scientifically flawed” because the proposed “functional acetate limitations are
not even commensurate in scope with the functions of the nucleic acid sequences
specifically recited in the disputed claim term.” (Pls.’ Reply (dkt. #97) 25-26.)6 As to
the remaining addition, DSM argues that the patentee actually noted that the patented
cell did grow preferentially with acetate, but that that statement was not a limitation
required by the claims but rather was prompted by a Lallemand corporate

6

Specifically, DSM argues that a yeast cell with only (EC 6.2.1.1) and alcohol dehydrogenase
activity (EC 1.1.1.1) (as specified in the term itself) cannot convert acetate to ethanol and that
the claimed cell’s ability to “consume acetate and create ethanol stems from the acetyl-Coenzyme
A synthetase and alcohol dehydrogenase activities in combination with the claimed acetylating
acetaldehyde dehydrogenase activity.” (Pls.’ Reply (dkt. #97) 25.)

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representative’s admission that the accused products consume acetate. (Pls.’ Opening Br.
(dkt. #59) 26-27.) DSM also argues that Lallemand’s construction defines the claimed
cells “in terms of how they might be used,” even though the claims do not contain that
requirement. (Pls.’ Reply (dkt. #97) 26.)
A patent’s prosecution history sheds light on how the inventor and the Patent and
Trademark Office conceptualized the patent. Phillips, 415 F.3d at 1317. Prosecution
disclaimer is a doctrine that prevents “patentees from recapturing through claim
interpretation specific meanings disclaimed during prosecution.” MIT, 839 F.3d at 1119
(quoting Omega Eng’g, Inc. v. Raytek Corp., 334 F.3d 1314, 1323 (Fed. Cir. 2003)).
However, the doctrine only applies where the patentee’s disavowal is “both clear and
unmistakable.” Id. (quoting 3M Innovative Props. Co. v. Tredegar Corp., 725 F.3d 1315,
1325 (Fed. Cir. 2013)). Anything short of “clear and unmistakable,” which must be
proved by the party attempting to invoke prosecution disclaimer, does not warrant
application of the doctrine. Id. This is a “high standard.” See id. at 1120.
Having reviewed the prosecution history, the court concludes that Lallemand has
not met this “high standard.”

Even without the addition of Lallemand’s proposed

limitations, the patented invention would not clearly be obvious. Indeed, the patentee
did not argue that these features were present in the invention in an attempt to
distinguish it from the prior art. Rather, the patentee argued that one of ordinary skill in
the art would not realize the benefits of production of acetate since Sonderegger and
Valadi tried to reduce the production of acetate and viewed that as a negative. Thus, the
invention actually teaches away from this prior art by making use of a formerly

13

disfavored enzyme.
Further, these additions are not scientifically necessary. Claim 1 provides for a
yeast cell that has three modifications: (1) a genetic modification to reduce the
production of GPD and/or GPP; (2) the addition of alcohol dehydrogenase (EC 1.1.1.1)
and acetyl-Coenzyme A synthetase (EC 6.2.1.1); and (3) the addition of acetylating
acetaldehyde dehydrogenase activity (EC 1.2.1.10). Without the second modification,
the yeast cells would not be able to function adequately because the only modification
would have been to delete GPD or GPP, meaning that the cells would not be able to use
glycerol production to achieve redox balance, thereby stymying the production of
ethanol.

In the invention, acetate is catalyzed to become acetyl-CoA, which in turn

permits the acetylating acetaldehyde dehydrogenase activity to produce ethanol, via
alcohol dehydrogenase. Thus, term 4 provides the clarification of acetate as the basis for
the redox reaction. Lallemand’s additional limitations therefore are not necessary.
Thus, the court construes this term to mean “the cells comprise (i) one or more
nucleic acid sequences encoding an acetyl-Coenzyme A synthetase activity (EC 6.2.1.1)
and (ii) one or more nucleic acid sequences encoding an NAD+-dependent alcohol
dehydrogenase activity (EC 1.1.1.1).”

Entered this 7th day of March, 2018.
BY THE COURT:
/s/
__________________________________
WILLIAM M. CONLEY
District Judge

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