11344992 (B.P.A.I. May. 13, 2011)

Ex Parte Elder et al

Board of Patent Appeals and InterferencesMay 13, 2011

11344992 (B.P.A.I. May. 13, 2011)

UNITED STATES PATENT AND TRADEMARK OFFICE UNITED STATES DEPARTMENT OF COMMERCE United States Patent and Trademark Office Address: COMMISSIONER FOR PATENTS P.O. Box 1450 Alexandria, Virginia 22313-1450 www.uspto.gov APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO. 11/344,992 02/01/2006 Vincent Allen Elder CFLAY.00332 9703 22858 7590 05/13/2011 CARSTENS & CAHOON, LLP 13760 NOEL ROAD, SUITE 900 DALLAS, TX 75240 EXAMINER THAKUR, VIREN A ART UNIT PAPER NUMBER 1782 MAIL DATE DELIVERY MODE 05/13/2011 PAPER Please find below and/or attached an Office communication concerning this application or proceeding. The time period for reply, if any, is set in the attached communication. PTOL-90A (Rev. 04/07) UNITED STATES PATENT AND TRADEMARK OFFICE _________________ BEFORE THE BOARD OF PATENT APPEALS AND INTERFERENCES _________________ Ex parte VINCENT ALLEN ELDER, JOHN GREGORY FULCHER, and HENRY KIN-HANG LEUNG Appellants. _________________ Appeal 2010-007704 Application 11/344,992 Technology Center 1700 _________________ Before RICHARD E. SCHAFER, SALLY GARDNER LANE, and MICHAEL P. TIERNEY, Administrative Patent Judges. LANE, Administrative Patent Judge. DECISION ON APPEAL Appeal 2010-007704 Application 11/344,992 2 The appeal, under 35 U.S.C. § 134, is from a Final Rejection of Appellants’ claims 27-38 and 45-85. Appellant canceled claims 1-26 and 39-441. (App. Br. 3.) We have jurisdiction under 35 U.S.C. § 6(b). We affirm. Appellant’s specification is directed to methods for reducing acrylamide in thermally processed foods. (Spec. 2.) Claim 27, a representative claim, recites: A method for the reduction of acrylamide formation in thermally processed foods comprising the steps of: (a) providing a food ingredient that contains asparagine; (b) inactivating asparagine in the asparagine-containing food ingredient by contacting the asparagine-containing food ingredient with asparaginase and a divalent cation; (c) using said food ingredient as a component in a food mixture; and (d) heating said food mixture to form a thermally processed food. (App. Br. 26, Claims App’x.) The Examiner rejected claims 27-37, 45-49, and 60-85 under 35 U.S.C. § 112, first paragraph, for lack of a supporting written description. (Ans. 9.) Appellants did not argue for the separate patentability of these claims. Accordingly, we focus on claim 27 in our review. See 37 C.F.R. § 41.37(c)(vii). 1 Appellants state in their Appeal Brief that claims 39-44 were cancelled in an amendment accompanying the Appeal Brief. (App. Br. 3.) Though we have not located in the record a separately filed amendment cancelling these claims, we rely upon Appellants’ statement that it has cancelled claims 39- 44 for purposes of deciding this appeal. Appeal 2010-007704 Application 11/344,992 3 The Examiner also rejected 11 groups of claims under 35 U.S.C. § 103(a) over the prior art, relying on numerous patent and printed publication documents. (Ans. 9-23.) A complete list of these patents and publications is available on pages 7-8 of the Examiner’s answer, including: Patton 2,448,152 August 13, 1948 White 5,368,879 November 29, 1994 Beck 5,389,389 February 14, 1995 Zyzak 2004/0058046 March 25, 2004 Barber et al., “Reversed-Phase High-Performance Liquid Chromatography Analysis of Changes in Free Amino Acids During Wheat Bread Dough Fermentation,” 66 Cereal Chem. 283-88 (1989) (“Barber”). Mottram et al., “Acrylamide is formed in the Maillard Reaction,” 419 Nature 448 (2002) (“Mottram”). Edwin C. Webb, Enzyme Nomenclature 1992: Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes (Academic Press 1992) 422 (“Enzyme Nomenclature”). Appellants did not provide separate arguments for individual claims rejected under 35 U.S.C. § 103. We focus on claim 27 in our review. See 37 C.F.R. § 41.37(c)(vii). The Examiner also rejected Appellants’ claims under the doctrine of obviousness-type double-patenting. (Ans. 23-30.) These rejections are provisional, being based on copending patent applications. Because a decision would be premature, we decline to address these rejections. See Ex parte Moncla, 95 USPQ2d 1884 (BPAI 2010). Appeal 2010-007704 Application 11/344,992 4 35 U.S.C. § 112, first paragraph The Examiner rejected Appellants’ claims for lack of written description under 35 U.S.C. § 112, first paragraph, finding that the Detailed Description of the Invention does not support using asparaginase and divalent cations together. (Ans. 9 and 31.) The Detailed Description of the Invention provides: One such method for inactivating is to contact asparagine with the enzyme asparaginase. . . . Asparagine may also be inactivated as the precursor of acrylamide in a thermally processed food by leaching. . . . Asparagine may further be inactivated as the precursor of acrylamide in a thermally processed food by fermentation. Asparagine can also be incorporated into proteins to inactivate asparagine as a precursor to acrylamide. Asparagine may be further inactivated as the precursor of acrylamide by the addition of a divalent cation such as calcium in the form of calcium lactate, calcium citrate or calcium malate. (Spec. p. 5, l. 16, through p. 6, l. 2 (emphasis added).) According to the Examiner, the specification only describes the recited methods for use individually. (Ans. 31.) The Examiner failed to find any other support in the specification, such as working examples, of using asparaginase and divalent cations together. (Id.) Appellants dispute this characterization of their specification, arguing that because the specification states asparagine can be “further inactivated” by adding divalent cation, it would reasonably have conveyed to those in the art that in addition to asparaginase, other asparagine-inactivating methods can be used, such as divalent cation. (App. Br. 13.) Appellants cite to a dictionary definition of “further” to mean “in addition.” (Id., see http://www.merriam-webster.com/dictionary/further.) Appeal 2010-007704 Application 11/344,992 5 “Compliance with the written description requirement of 35 U.S.C. § 112, ¶ 1 is a question of fact . . . .” Centocor Ortho Biotech, Inc. v. Abbott Labs., 97 U.S.P.Q.2d 1870, 1874 (Fed. Cir. 2011). It is reasonable that those of skill in the art would read the word “further” in Appellants’ written description to mean that more inactivation, in addition to that accomplished with asparaginase alone, can be achieved by adding a divalent cation. Accordingly, we reverse the rejection under 35 U.S.C. § 112, first paragraph. 35 U.S.C. § 103 The Examiner relies on Mottram and White to show knowledge of the “Maillard Reaction,” which involves asparagine and produces acrylamide. (See Mottram, right col., last paragraph; see also White, col. 4, ll. 34-50.) Further, the Examiner relies on Zyzak, Barber, and Enzyme Nomenclature to show that those in the art knew of methods to reduce asparaginase and that such reduction would limit the effects of the Maillard reaction and, thus, acrylamide production. (See Zyzak, ¶ [0018]; Barber, p. 283, left col., last paragraph; and Enzyme Nomenclature, p. 422.) Appellants argue that White and Zyzak teach away from the claimed method of reducing acrylamide because they teach that hydrolysis of asparagine with asparaginase produces aspartic acid (see Zyzak, Fig. 2; see also Enzyme Nomenclature, p. 422) and that aspartic acid acts like asparagine to cause browning, and thus acrylamide production, through the Maillard reaction (see White, col. 4, ll. 34-52). (App. Br. 15-18.) For example, White teaches Conditions provided during the process of the present invention most desirably are such that certain components of the steak sauce extract undergo Maillard or Browning Reactions. Such reactions are reactions between (i) the amino substituents of amino acids, peptides, Appeal 2010-007704 Application 11/344,992 6 proteins or other nitrogen-containing compounds, and (ii) the carbonyl group of a sugar in the reducing form or other carboxyl-containing compounds. . . . Exemplary amino acids include asparagine . . . aspartic acid . . . and the like. (White, col. 4, ll. 34-52.) According to Appellants, these teachings indicate that those in the art would not have had a reason to use aparaginase because it would only result in “‘trad[ing]’ one Maillard reactant (e.g., asparagine) for another (e.g., aspartic acid).” (App. Br. 16.) “Under the proper legal standard, a reference will teach away when it suggests that the developments flowing from its disclosures are unlikely to produce the objective of the applicant's invention.” Syntex LLC v. Apotex, Inc., 407 F.3d 1371, 1380 (Fed. Cir. 2005). Though the prior art teaches that both asparagine and aspartic acid act in the Maillard reaction, as Appellants acknowledge, the claimed method would produce aspartic acid. (See Appellants’ claim 45 (“(b) reacting the asparagine in the asparagine- containing food ingredient with an enzyme asparaginase and a divalent cation, wherein said asparaginase consists essentially of the enzyme, thereby producing aspartic acid and ammonia . . . .” App. Br. 28, Claims App’x.). Appellants do not provide persuasive argument or evidence that merely because aspartic acid is produced, those of skill in the art would have considered asparaginase to be unlikely to reduce acrylamide production overall or would otherwise have been discouraged from using asparaginase to reduce acrylamide production. Thus, we are not persuaded that White’s teaching of aspartic acid as a reactant for the Maillard reaction teaches away from the claimed method Appeal 2010-007704 Application 11/344,992 7 The Examiner cites Beck as teaching that exposure to calcium chloride minimizes browning when fruits and vegetables, including potatoes, are subsequently processed. (Ans. 10-11; Beck, abstract, col. 5, ll. 1-7.) Appellants argue that, in contrast, those in the art would not have had a reason to add calcium chloride because Patton teaches the calcium ions do not react with the browning reactants, but merely prevent the extraction of non-browning substances needed for texture and flavor. (App. Br. 18 and 21, see Patton, col. 3, ll. 66-71.) Appellants also argue that if calcium chloride was used as a leaching agent, there would not have been a reason to add asparaginase because all of the reactants would have been removed. (App. Br. 18.) Patton teaches removing browning reactants by immersing potato in calcium chloride. (Patton, col. 2, ll. 17-23.) Though Patton teaches that the calcium ions do not react with browning reactants, it adds the proviso that this is “so far as known.” (Patton, col. 3, ll. 66-67.) Patton reflects the state of the art in 1948, when Patton was issued. Later, in 1995, when Beck was issued, those in the art learned that calcium chloride is a discoloration inhibitor. (Beck, abstract: “Methods for treating produce to minimize browning upon subsequent processing, handling and/or storage when the processing involves exposing produce . . . particularly potatoes, to discoloration inhibitors including . . . calcium chloride . . . .”; see also Beck col. 5, ll. 1-7.) Appellants have not persuaded us that despite the uncertainty at the time Patton was issued, those in the art at the time Appellants filed Appeal 2010-007704 Application 11/344,992 8 their application,2 would not have known to use calcium chloride to reduce browning. Accordingly, we are not persuaded that those in the art would not have used both asparaginase and divalent cation, such as calcium chloride, to reduce acrylamide production. ORDER The Examiner’s rejection under 35 U.S.C. § 112, first paragraph, is REVERSED. The Examiner’s rejections under 35 U.S.C. § 103(a) over the prior art, are AFFIRMED. AFFIRMED KMF 2 The current application was filed on February 1, 2006, and was based as a continuation on an application filed September 19, 2002.