Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Detailed Action
This office action is in response to applicant’s communication filed on 7/20/26.
Claims 1-8 are pending in this application and are being examined in this Office Action.
Applicant's election of Group I, claims 1 and 4-8, without traverse, in the reply filed on is acknowledged. Thus claims 2-3 are withdrawn from consideration being drawn to the non-elected invention. As a result, claims 1 and 4-8 are being examined in this Office Action.
Priority
The applicant claims benefit as follows:
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Objections
Claim 6 is objected to because of the following informalities:
Claim 6 recites both "dialdehyde oxalate" and "glyoxal (dialdehyde oxalate)" in the same Markush group. These are the same compound, as the compound within the parenthesis shows. One compound cannot be two members of one group. One of the two recitations should be deleted.
Claim 6 recites "(Z)-7-hexadesenal." No such compound is known. The compound appears to be (Z)-7-hexadecenal.
Claim 6 recites "1-naphthoaldehyde." Paragraph [0081] of the specification recites "1-naphthaldehyde" for the same compound. The claim and the specification should agree.
Reference to applicant’s specification within this office action refers to applicant’s PGPub: US 20240093251
Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(a):
(b) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
Claims 1 and 4-8 are rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement.
Claim 1 recites that the biocatalyst "comprises cells or bacterial cells containing nitrile hydratase." Given the broadest reasonable interpretation, "cells" is not limited to bacterial cells. Paragraph [0038] states that "an animal cell, a plant cell, an organelle or a bacterial cell containing nitrile hydratase and a processed material thereof may be used." Claim 1 therefore covers methods using animal cells, plant cells or organelles containing nitrile hydratase.
The specification does not describe a representative number of species of this genus. It also does not disclose structural features common to the genus. Every working example uses bacterial cells. Example 1 and Test Example 1 use Rhodococcus rhodochrous J-1 (FERM BP-1478). Example 5 uses a Rhodococcus rhodochrous ATCC 12674 transformant expressing nitrile hydratase of Rhodococcus rhodochrous M8. Example 6 uses a Rhodococcus rhodochrous ATCC 12674 transformant expressing nitrile hydratase of Pseudonocardia thermophila JCM3095. The lists of biocatalyst sources at paragraphs [0043] and [0044] are all bacterial. No animal cell, plant cell or organelle containing nitrile hydratase is named anywhere in the specification.
Thus, applicant was not in possession of the full scope of the claimed subject matter as of the effective filing date. See Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1350 (Fed. Cir. 2010) (en banc) and MPEP 2163. Claims 4-8 are rejected for the same reason as depending from claim 1. Amending claim 1 to recite "bacterial cells containing nitrile hydratase" would overcome this rejection.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
Claims 1 and 4-8 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112, second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor regards as the invention.
Claim 1 is indefinite because the claim recites that the biocatalyst "comprises cells or bacterial cells containing nitrile hydratase." Bacterial cells are cells. The claim thus offers a genus and one of its own species as alternatives. It is unclear whether "cells" carries its full meaning, or whether "cells" is meant to exclude bacterial cells. The metes and bounds of the limitation are unclear. Claims 4-8 are rejected as depending from claim 1.
Claim 4 is indefinite because the claim recites "a concentration of a cyan compound in the nitrile compound." The term "cyan compound" is not a term of art. Paragraph [0091] states that "examples of the cyan compound include compounds containing cyan or releasing cyan or a cyan ion in a reaction condition, such as hydrocyanic acid (HCN), cyanide ion (CN-), sodium cyanide and potassium cyanide." That statement is circular and open ended. It is not an adequate definition. Acrylonitrile, acetonitrile, methacrylonitrile, cyanopyridine, glycolonitrile and alanine nitrile each contain a cyano group. It is therefore unclear whether the nitrile compound of claim 1 is itself a "cyan compound" for purposes of the recited ratio. Under that reading the claimed ratio and the claim scope would be entirely different.
Claim 4 is further indefinite because the recited ratio has no antecedent basis and thus cannot always be computed. Claim 1 does not require any cyan compound to be present. Where no cyan compound is present, the ratio is undefined, and it cannot be determined whether the embodiment falls inside or outside the claim.
Claim 4 is further indefinite because it is unclear where the recited concentrations are measured. Claim 4 measures the cyan compound "in the nitrile compound." Paragraph [0087] instead states that "the amount (molar ratio) of an aldehyde compound to be added in a reaction solution relative to the content of a cyan compound in the reaction solution is set at 0.9 to 15." The claim does not state where the aldehyde concentration is measured at all.
Claim 5 is indefinite because it conflicts with the claim from which it depends. Claim 1 requires that the biocatalyst "comprises cells or bacterial cells containing nitrile hydratase." Claim 5 requires that the biocatalyst "is nitrile hydratase derived from the genus Rhodococcus or Pseudonocardia; or cells, bacterial cells, or a processed material thereof containing the nitrile hydratase." The first alternative of claim 5 is the enzyme alone. The third alternative is a processed material. Neither requires cells. It is unclear whether claim 5 requires cells or allows their absence.
Claim 7 is indefinite because its Markush group conflicts with the group of the claim from which it depends. Claim 1 requires the nitrile compound to be selected from acrylonitrile, acetonitrile, methacrylonitrile, cyanopyridine, glycolonitrile and alanine nitrile. Claim 7 recites acrylonitrile, acetonitrile, methacrylonitrile, cyanopyridine, glycolonitrile and lactonitrile. Claim 7 thus adds lactonitrile, which claim 1 excludes, and drops alanine nitrile, which claim 1 includes. It cannot be determined whether an embodiment using lactonitrile alone falls within claim 7.
Claim 8 is indefinite because the claim recites a "catalyst composition comprising: an aldehyde compound and a biocatalyst having nitrile hydratase activity." An aldehyde compound is a reagent, not a catalyst. The specification does not say what separates the recited "catalyst composition" from the ordinary reaction mixture already required by claim 1, in which the aldehyde compound and the biocatalyst are both present. It cannot be determined what the term requires.
Appropriate correction is required.
The following is a quotation of 35 U.S.C. 112(d):(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 5, 7 and 8 are rejected under 35 U.S.C. 112(d) as being of improper dependent form for failing to further limit the subject matter of the claim upon which they depend.
Claim 5 does not further limit claim 1. Claim 1 requires the biocatalyst to comprise cells or bacterial cells containing nitrile hydratase. Claim 5 allows the biocatalyst to be the nitrile hydratase enzyme alone, without cells. Claim 5 also allows the biocatalyst to be "a processed material thereof." Both alternatives are broader than claim 1. A dependent claim that broadens its parent does not further limit it. Applicant may cancel the claim, amend it to proper dependent form, or rewrite it in independent form.
Claim 7 does not further limit claim 1 to the extent it allows lactonitrile to be the nitrile compound. Lactonitrile is excluded from the group of claim 1. To that extent claim 7 recites subject matter outside the scope of claim 1.
Claim 8 does not further limit claim 1. Claim 1 already requires the amide compound to be produced both "in the presence of a biocatalyst having nitrile hydratase activity" and "in the presence of an aldehyde compound." Claim 8 requires only that the production be carried out "by using a catalyst composition comprising an aldehyde compound and a biocatalyst having nitrile hydratase activity." Given the broadest reasonable interpretation, once the aldehyde compound and the biocatalyst are both present, as claim 1 requires, a composition comprising the two necessarily exists and the production is necessarily carried out using it. Claim 8 thus adds no limitation not already in claim 1.
Appropriate correction is required.
Claim Rejections – 35 USC 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of the AIA 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1 and 4-8 are rejected under 35 U.S.C. 102(a)(1) and/or 102(a)(2) as being anticipated by Pierce (WO 9827016, pub date 06/25/1998, in applicant’s IDS filed 8/1/2025, the US equivalent US 6132985, pub date Oct. 17, 2000, is used herein).
Pierce teaches a method for detoxifying a mixture of nitrile compounds. The method comprises contacting a pure culture of an induced microorganism strain with the mixture for a time sufficient to convert the nitriles to the corresponding amides. Pierce teaches that detoxification of a nitrile includes its conversion to the corresponding amide. Pierce further teaches that the microorganisms that convert a nitrile to the corresponding amide contain nitrile hydratase enzyme activity. (Pierce, column 8, lines 52-58; column 10, lines 52-58; column 26, lines 1-6)
Pierce teaches that the microorganism strains used are Rhodococcus rhodochrous strain DAP 96622 and Rhodococcus sp. strain DAP 96253. Pierce teaches that these strains are used as whole cells, which are harvested, centrifuged and washed with phosphate buffered saline before use. (Pierce, column 18, lines 12-25; column 34, lines 28-36; column 38, lines 12-18)
Pierce teaches at Example 6 that multiply induced whole cells of Rhodococcus sp. strain DAP 96253 were contacted at 25 degrees C with a test mixture containing 164 ppm acrylonitrile, 160 ppm acetonitrile, 51 ppm acrylamide, 54 ppm acrolein, 51 ppm fumaronitrile and 102 ppm succinonitrile. Pierce teaches in the footnote to Table XII that acetamide was not initially present in the test mixture but was formed by conversion of acetonitrile. Pierce teaches the same test mixture, reported as containing 53.5 ppm acrolein, at Section 8.2 with induced whole cells of Rhodococcus rhodochrous strain DAP 96622 and at Example 9 with induced whole cells of Rhodococcus sp. strain DAP 96253. (Pierce, column 34, lines 36-48; column 35, Table XII and footnote; column 37, lines 1-9; column 38, lines 12-25)
Pierce teaches that a Wastewater Column Bottom (WWCB) from an acrylonitrile production plant using the SOHIO process contains approximately 1230 mg/l acrylonitrile, 4500 mg/l acetonitrile, 1490 mg/l acrylamide, 1070 mg/l acrolein, 547 mg/l succinonitrile, 1446 mg/l fumaronitrile and 335 mg/l total cyanide. Pierce teaches at Example 10 that this WWCB, at full strength and supplemented with 200 ppm each of acrylonitrile and acetonitrile, was detoxified using induced whole cells of Rhodococcus rhodochrous strain DAP 96622. (Pierce, column 28, lines 43-53; column 38, lines 34-62)
Regarding claim 1, Pierce teaches a method for producing an amide compound from a nitrile compound in the presence of a biocatalyst having nitrile hydratase activity. Pierce teaches that the amide compound is produced from the nitrile compound in the presence of an aldehyde compound, namely 54 ppm acrolein. Pierce teaches that the nitrile compounds are acrylonitrile and acetonitrile, each of which is a member of the group recited in claim 1. Pierce teaches that the biocatalyst comprises cells or bacterial cells containing nitrile hydratase, namely whole cells of the induced Rhodococcus strain. (Pierce, column 10, lines 52-58; column 34, lines 36-48; column 35, Table XII and footnote)
With regard to claim 4, Pierce teaches a WWCB containing 1070 mg/l acrolein and 335 mg/l total cyanide, and teaches at Example 10 that this WWCB is detoxified at full strength with induced whole cells of Rhodococcus rhodochrous strain DAP 96622. On these values the acrolein content is 1070 mg/l divided by 56.06 g/mol, or 19.09 mmol/l. The total cyanide content is 335 mg/l divided by 26.02 g/mol, or 12.88 mmol/l as cyanide ion. The ratio of the aldehyde compound to the cyan compound is thus 1.48 by a molar ratio. Calculated instead as hydrocyanic acid, the cyanide content is 12.40 mmol/l and the ratio is 1.54. On either basis the ratio falls within the recited range of from 0.9 to 15. (Pierce, column 28, lines 43-53; column 38, lines 34-62)
Pierce states that the WWCB acrolein is present "in the form of acrolein cyanohydrin." That statement does not remove the acrolein from the scope of "an aldehyde compound." Paragraph [0082] of the specification states that aldehyde compounds include "compounds producing an aldehyde compound in water or in a solution," and paragraph [0123] states that the recited ratio is computed for such compounds on the molar number of the aldehyde formed in water. Further, the acrolein content of 19.09 mmol/l exceeds the total cyanide content of 12.88 mmol/l. Because one mole of cyanide is consumed per mole of aldehyde, at most 12.88 mmol/l of the acrolein can be bound as the cyanohydrin. Not less than 6.21 mmol/l is therefore present as the free aldehyde. (Pierce, column 28, lines 43-53; applicant's specification, paragraphs [0082] and [0123])
With regard to claim 5, Pierce teaches that the biocatalyst is whole cells of Rhodococcus rhodochrous strain DAP 96622 and of Rhodococcus sp. strain DAP 96253. These are bacterial cells containing nitrile hydratase derived from the genus Rhodococcus. (Pierce, column 18, lines 12-25; column 38, lines 12-25 and 34-62)
With regard to claim 6, Pierce teaches that the aldehyde compound present is acrolein. Acrolein is recited in the Markush group of claim 6. (Pierce, column 34, lines 36-48; column 38, lines 12-25)
With regard to claim 7, Pierce teaches that the production of the amide compound is carried out using a composition comprising an aldehyde compound and at least one nitrile compound of the recited group. The test mixture of Example 6 comprises acrolein, acrylonitrile and acetonitrile. The WWCB of Example 10 likewise comprises acrolein, acrylonitrile and acetonitrile. (Pierce, column 28, lines 43-53; column 34, lines 36-48; column 38, lines 34-62)
With regard to claim 8, Pierce teaches that the production of the amide compound is carried out using a composition comprising an aldehyde compound and a biocatalyst having nitrile hydratase activity. The induced whole cells and the acrolein-containing mixture are combined in one aqueous reaction medium. (Pierce, column 34, lines 36-48; column 38, lines 12-25 and 34-62)
Therefore these claims are fully met.
Claims 1 and 6-8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Amarant et al. ("Substrates and Inhibitors of the Nitrile Hydratase and Amidase of Corynebacterium nitrilophilus," Biotechnology and Applied Biochemistry, Vol. 11, No. 1, pages 49-59, 1989, in applicant’s IDS filed 08/01/2025).
Amarant et al. teaches that Corynebacterium nitrilophilus (ATCC 21419) produces a nitrile hydratase which hydrates nitriles to amides. Amarant et al. teaches that the enzymes were studied in the whole bacterial cells as well as in the cell free extract, and that no difference was detected in their enzymatic properties. Amarant et al. teaches that the harvested cells, assayed intact, showed an activity of 5 plus or minus 1 U of hydratase per mg dry weight using acrylonitrile as substrate. (Amarant et al., page 49, abstract; page 50, left and right columns)
Amarant et al. teaches that aldehydes do not affect the activity of the nitrile hydratase, and that the hydratase retained full activity when assayed in the presence of 0.5 to 5 mM acetaldehyde. Amarant et al. teaches that acetaldehyde at a final concentration of 2 mM was routinely added to reaction mixtures whenever conversion of nitriles to amides was desired. (Amarant et al., page 49, abstract; page 55, right column)
Amarant et al. teaches at Table IV that a solution containing 50 mM acrylonitrile in 0.1 M phosphate buffer at pH 7 was mixed with dried cells at 2 units/ml and incubated at 36 degrees C, with and without 2 mM acetaldehyde. Amarant et al. teaches that the conversion of acrylonitrile to acrylamide with 2 mM acetaldehyde was 74.2 percent at 0.25 hours, 100.0 percent at 0.5 hours and 95.0 percent at 18 hours. Amarant et al. teaches that dried whole cells were incubated and assayed in the presence of 2 mM acetaldehyde or of 5 mM propionaldehyde. (Amarant et al., page 55, right column; page 56, Table IV)
Regarding claim 1, Amarant et al. teaches a method for producing an amide compound from a nitrile compound in the presence of a biocatalyst having nitrile hydratase activity. Amarant et al. teaches that acrylamide is produced from acrylonitrile in the presence of an aldehyde compound, namely 2 mM acetaldehyde. Acrylonitrile is a member of the group recited in claim 1. Amarant et al. teaches that the biocatalyst comprises cells or bacterial cells containing nitrile hydratase, namely dried whole cells of Corynebacterium nitrilophilus. (Amarant et al., page 50, left and right columns; page 56, Table IV)
With regard to claim 6, Amarant et al. teaches that the aldehyde compound is acetaldehyde. Acetaldehyde is recited in the Markush group of claim 6. (Amarant et al., page 55, right column; page 56, Table IV)
With regard to claim 7, Amarant et al. teaches that the production of the amide compound is carried out using a composition comprising an aldehyde compound and at least one nitrile compound of the recited group. The reaction solution of Table IV comprises 2 mM acetaldehyde and 50 mM acrylonitrile. (Amarant et al., page 56, Table IV)
With regard to claim 8, Amarant et al. teaches that the production of the amide compound is carried out using a composition comprising an aldehyde compound and a biocatalyst having nitrile hydratase activity. The dried whole cells and the acetaldehyde are combined in the reaction solution of Table IV. (Amarant et al., page 55, right column; page 56, Table IV)
Therefore these claims are fully met.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Jennifer Cho Sawyer whose telephone number is (571) 270 1690. The examiner can normally be reached on Monday-Friday 9 AM - 6 PM PST.
If attempts to reach the examiner by telephone are unsuccessful, the examiner's supervisor, Renee Claytor can be reached on (571) 272-8394. The fax phone number for the organization where this application or proceeding is assigned is 571-274-1690.
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/JENNIFER C SAWYER/Examiner, Art Unit 1691
/RENEE CLAYTOR/Supervisory Patent Examiner, Art Unit 1691
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