DETAILED ACTION
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 .
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claim(s) 1, 3, 5-8 and 15-17 are rejected under 35 U.S.C. 103 as being unpatentable over Van Der Maarel et al (WO 03/002728 A2) in view of Melim Miguel et al (Enzymes in Bakery: Current and Future Trends).
In regard to claims 1 and 15-17, Van Der Maarel et al discloses:
Also, the invention provides use such a polypeptide or fragment in hydrolysing starch, said uses for example applied in the prevention or at least temporarily avoiding of staling of bakery products such as bread, or as a replacement of acid hydrolysis in the production of starch hydrolysates. Such prevention of staling comprises use of a method for reducing retrogradation of starch comprising treating said starch with a polypeptide or fragment, such as a amylomaltase or branching enzyme provide with hydrolysing activity according to the invention. Improved quality of baked products is further obtained when the alpha-glucanotransferase (e.g. amylomaltase or branching enzyme) provided with hydrolysing activity according to the invention is used in combination with other enzymes, such as a-amylase, maltogenic amylase, cyclodextrin glycosyltransferase, beta-amylase, cellulase, oxidase and/or lipase. Furthermore, the invention provides a bakery ingredient comprising a polypeptide according to the invention and a bakery product such as bread comprising a polypeptide according to the invention. The invention is further explained in the detailed description provided herewith (page 17 lines 9-16).
In regard to claims 1 and 3, Van Der Maarel et al further discloses that amylomaltase is obtained from Thermus thermophilus, Thermus aquaticus or Aquifex aeolicus:
The complete lack of hydrolyzing activity of wild type AMase and its specificity for donor and acceptor substrates makes it a very interesting enzyme to be studied regarding reaction and product specificity.
In another embodiment, the invention provides a nucleic acid encoding a enzyme or polypeptide derived from said non-hydrolysing enzyme, now provided with hydrolysing acitivity. For example, interaction with hydrophobic amino acids, such as F366, which is highly conserved in amylomaltases, is involved in the reaction specificity of the enzyme. Hydrolyzing activity can be introduced by mutating this residue, or other hydrophobic residues such as F251 or Y54. This hydrolyzing activity has significant effects on product profiles of the enzyme, indicating the necessity of complete absence of hydrolysis for the function of the wild type enzyme (the production of longer oligosaccharides from short substrates). Now that the enzyme has been provided with hydrolysing activity, it can be used in preventing retrogradation of starch. Especially useful in such prevention is the use of a newly hydrolising enzyme as provided herein that is derived from thermostable transferase, which can be found in a thermophilic micro-organism. Particulary provided is such an enzyme wherein said micro-organism comprises Thermus thermophilus, Thermus aquaticus or Aquifex aeolicus (page 14).
Hence, Van Der Maarel et al further discloses improvement in quality of baked products is further obtained when the amylomaltase obtained from Thermus thermophilus, Thermus aquaticus or Aquifex aeolicus provided with hydrolysing activity according to the invention is used in combination with other enzymes, such as a-amylase, maltogenic amylase, cyclodextrin glycosyltransferase, beta-amylase, cellulase, oxidase and/or lipase.
Van Der Maarel et al does not disclose additional enzymes as recited in claims 1, 6-7, and 15-17.
Melim Miguel et al discloses application of enzymes in bakery. Melim Miguel et al discloses “Enzymes are an important ingredient used in most bakery products. More recently enzymes have assumed an even greater importance in baking, due to the restrictions on the use of chemical additives, especially in the manufacture of bread and other fermented products” (1. Introduction).
In regard to baking, starch and baked products, Melim Miguel et al discloses:
Baking is a common name for the production of baked goods, such as bread, cake, pastries, biscuits, crackers, cookies, pies and tortillas, where wheat flour is both the most essential ingredient and key source of enzyme substrates for the product [12]. Even though based on cereals other than wheat, baked goods such as gluten-free products or rye bread are also considered to be baked products [8]. Baked goods formulations vary significantly depending on the desired final product, and typical ingredients, apart from starch, can include wheat flour (8-16% protein, 71-79% carbohydrate), fats, sugars, eggs, emulsifiers, milk and/or water [13].
Bread is usually made from wheat flour as raw material, which is a mixture of starch, gluten, lipids, non-starch polysaccharides and enzymes. After flour, yeast and water are mixed, complex biochemical and biophysical processes begin, catalyzed by the wheat enzymes and by the yeast, characterizing the dough phase. These processes go on in the baking phase, giving rise to bread. Extra enzymes added to the dough improve control of the baking process, allowing the use of different baking processes, reducing process time, slowing-down staling, compensating for flour variability and substituting chemical additives [14]. Starch is the main component of products such as bread and other bakery goods and is added to different foods, acting as a thickener, water binder, emulsion stabilizer, gelling agent and fat substitute [15]. It is the most abundant constituent and most important reserve polysaccharide of many plants, including cereals, occurring as intracellular, semi-crystalline granules (section 3. Main Constituents of Baked Products).
In regard to enzymes used in baked products, Melim Miguel et al discloses:
The supplementation of flour and dough with enzyme improvers is a usual practice for flour standardization and also as baking aids. Enzymes are usually added to modify dough rheology, gas retention and crumb softness in bread manufacture, to modify dough rheology in the manufacture of pastry and biscuits, to change product softness in cake making and to reduce acrylamide formation in bakery products [8]. The enzymes can be added individually or in complex mixtures, which may act in a synergistic way in the production of baked goods [60-62], and their levels are usually very low (section 5. Enzymes used in baked products).
Further in regard to additional enzymes as recited in claims 1 and 15-17, Melim Miguel et al discloses:
Proteases can be subdivided into two major groups according to their site of action: exopeptidases and endopeptidases. Exopeptidases cleave the peptide bond proximal to the amino or carboxy termini of the substrate, whereas endopeptidases cleave peptide bonds distant from the termini of the substrate [77]. Most of the proteolytic activity of wheat and rye flours corresponds to aspartic proteases and carboxypeptidases, which are both active in acid pH. Additionally, aspartic proteases of wheat are partly associated with gluten [78]. Nevertheless, the proteolytic activity of sound, ungerminated grain is normally low [79].
Proteases are used on a large commercial scale in the production of bread, baked goods, crackers and waffles [80]. These enzymes can be added to reduce mixing time, to decrease dough consistency, to assure dough uniformity, to regulate gluten strength in bread, to control bread texture and to improve flavour [16,60]. In addition, proteases have largely replaced bisulfite, which was previously used to control consistency through reduction of gluten protein disulfide bonds, while proteolysis breaks down peptide bonds. In both cases, the final effect is a similar weakening of the gluten network [79].
In bread production, a fungal acid protease is used to modify mixtures containing high gluten content. When proteases are mixed in the blend, it undergoes partial hydrolysis becoming soft and easy to pull and knead [7,60]. Proteases are also frequently added to dough preparations. These enzymes have great impact on dough rheology and the quality of bread possibly due to effects on the gluten network or on gliadin [7].
Proteases are also applied in the manufacture of pastries, biscuits and cookies. They act on the proteins of wheat flour, reducing gluten elasticity and therefore reducing shrinkage of dough or paste after moulding and sheeting [8,81]; for instance, hydrolysis of glutenin proteins, which are responsible for the elasticity of dough, has considerable improving effects on the spread ratio of cookies [81] (section 5.1.2 Proteases).
Further in regard to additional enzymes as recited in claims 1 and 15-17, Melim Miguel et al discloses asparaginase and transglutaminase:
Among the enzymes which have attracted attention for use in bakery is asparaginase. Differently from other enzymes, its use is not associated with improved bread volume, crumb softening or reduced staling. Instead, asparaginase is claimed to have a high potential of reducing formation of acrylamide during baking [136-138]. Asparaginase (L-asparagine amidohydrolases, EC 3.5.1.1) catalyses the hydrolysis of asparagine to aspartic acid and ammonium, removing the precursor of acrylamide formation [139]. Acrylamide, classified as a probable human carcinogen, is formed in heated foods via Maillard reaction between asparagine and a carbonyl source [137,138,140,141]. Although asparaginase can be found among living organisms, including animals, plants and microorganisms, filamentous fungi as Aspergillus oryzae and A. niger have been explored for enzyme preparation aiming commercial purposes [142-144].
Transglutaminases (EC 2.3.2.13) from microbial sources also have potential for application in bakery products. Food proteins can be modified through cross-linking by transglutaminases, resulting in textured products, protecting lysine in food proteins from undesired chemical reactions, encapsulating lipids and lipid-soluble materials, forming heat and water resistant films, improving elasticity and water-holding capacity, modifying solubility and functional properties, and producing food proteins of higher nutritive value [29,145-153] (section 5.3 Other enzymes).
In the summary of the main application of different enzymes, Melim Miguel et al discloses:
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Both references are directed to the improvement of bread quality. Van Der Maarel et al discloses improvement in quality of baked products is further obtained when the amylomaltase obtained from Thermus thermophilus, Thermus aquaticus or Aquifex aeolicus provided with hydrolysing activity according to the invention is used in combination with other enzymes, such as oxidase and/or lipase. Melim Miguel et al discloses application of enzymes in bakery. Melim Miguel et al discloses use of protease, transglutaminase, asparaginase, phospholipase, glucoamylase and amyloglucosidase in baking in order to improve bread qualities such as:
Generation of fermentable compounds;
Increase in bread volume;
Reduction in fermentation time;
Improvement in dough viscosity, rheology and bread softness;
Improvement in bread texture;
Formation of reducing sugars and subsequent Maillard reaction products, intensifying bread flavor and color;
Decrease of bread crumb firming rate;
Anti-staling effects;
Reduction of dough mixing time;
Control of dough rheology or viscoelastic properties of gluten strength in bread;
Enhance dough extensibility;
Increase loaf or bread volumes;
Formation of aminoacids and flavors;
Crispness feature on bread crust;
Production of gluten-free products;
Cross-link between gluten and other peptides, forming a new protein network;
Increase volume and improve structure of breads, better retention of gas;
Improve bread crumb strength, height increase in puff pastry and croissants volume;
Improve dough stability;
Improve properties of gluten-free breads;
Protect frozen doughs from damage.
One of ordinary skill in the art would have been motivated to modify Van Der Maarel et al in view of Melim Miguel et al and to further employ additional enzymes as recited in claims 1, 6-7, and 15-17 for bread improvement as suggested by Melim Miguel et al. i.e. for the generation of fermentable compounds; increase in bread volume; reduction in fermentation time; improvement in dough viscosity, rheology and bread softness; improvement in bread texture; formation of reducing sugars and subsequent Maillard reaction products, intensifying bread flavor and color; decrease of bread crumb firming rate; anti-staling effects; reduction of dough mixing time; control of dough rheology or viscoelastic properties of gluten strength in bread; enhance dough extensibility; increase loaf or bread volumes; formation of aminoacids and flavors; crispness feature on bread crust; production of gluten-free products; cross-link between gluten and other peptides, forming a new protein network; increase volume and improve structure of breads, better retention of gas; improve bread crumb strength, height increase in puff pastry and croissants volume; improve dough stability; improve properties of gluten-free breads; protect frozen doughs from damage. Van Der Maarel et al already discloses combination of amylomaltase of the genus Thermus in combination with additional enzymes for bread quality improvement. Therefore to employ additional enzymes as recited in claims 1, 6-7, and 15-17 for the same purpose and function of bread quality improvement as suggested by Melim Miguel et al would have been obvious.
In regard to claim 1 and 15-17, one of ordinary skill in the art would have been motivated to vary the particular amount of amylomaltase based on the desired effect of improvement in quality of baked products.
Further in regard to the concentration recitations, it is noted that:
Generally, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235(CCPA 1955) (MPEP 2144.05, II A).
In regard to claim 3, Van Der Maarel et al further discloses that amylomaltase is obtained from Thermus thermophilus, Thermus aquaticus or Aquifex aeolicus (page 14).
In regard to claim 5, it is noted that claim 5 further limits starch degradation product recitation of claim 1, which is an optional limitation that is not required by claims 1 or 5.
In regard to claims 6 and 7, Melim Miguel et al discloses glucose oxidase:
Glucose oxidase (β-D-glucose:oxygen: 1-oxidoreductase; EC 1.1.3.4) catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone and hydrogen peroxide [118,119]. This enzyme has been obtained from different fungal sources, mainly from genus Aspergillus and Penicillium, being Aspergillus niger the most commonly used [120-123].
Glucose oxidase has been used successfully to remove residual glucose and oxygen in foods and beverages aiming to increase their shelf life. The hydrogen peroxide generated by this enzyme presents antimicrobial properties, and is easily removed by catalase utilization, which is an enzyme that catalyzes the conversion of hydrogen peroxide to oxygen and water [12,124-127]. Glucose oxidase can be used as alternative oxidizing agent instead of potassium bromate in breadmaking. Potassium bromate is an oxidizing agent that was traditionally used in baking, and its use was prohibited in many countries after it was recognized as carcinogenic [128,129] (Section 5.2.2 Glucose oxidase).
In regard to claim 8, Van Der Maarel et al discloses bakery products such as bread (page 17 lines 9-16).
Response to Arguments
Applicant's arguments filed 08/11/2025 have been fully considered but they are not persuasive.
Claim(s) 1-3, 5-8 and 15-17 are rejected under 35 U.S.C. 103 as being unpatentable over Van Der Maarel et al (WO 03/002728 A2) in view of Melim Miguel et al (Enzymes in Bakery: Current and Future Trends) for the reasons as stated immediately above. Another prior art reference to Melim Miguel et al was made as a teaching of use of protease, transglutaminase, asparaginase, and amyloglucosidase in baking in order to improve bread qualities.
Further in response to Applicant arguments, it is noted that:
Prima Facie Obviousness Is Not Rebutted by Merely Recognizing Additional Advantages or Latent Properties Present But Not Recognized in the Prior Art
Mere recognition of latent properties in the prior art does not render nonobvious an otherwise known invention. In re Wiseman, 596 F.2d 1019, 201 USPQ 658 (CCPA 1979) (Claims were directed to grooved carbon disc brakes wherein the grooves were provided to vent steam or vapor during a braking action. A prior art reference taught noncarbon disc brakes which were grooved for the purpose of cooling the faces of the braking members and eliminating dust. The court held the prior art references when combined would overcome the problems of dust and overheating solved by the prior art and would inherently overcome the steam or vapor cause of the problem relied upon for patentability by applicants. Granting a patent on the discovery of an unknown but inherent function (here venting steam or vapor) “would remove from the public that which is in the public domain by virtue of its inclusion in, or obviousness from, the prior art.” 596 F.2d at 1022, 201 USPQ at 661.); In re Baxter Travenol Labs., 952 F.2d 388, 21 USPQ2d 1281 (Fed. Cir. 1991) (Appellant argued that the presence of DEHP as the plasticizer in a blood collection bag unexpectedly suppressed hemolysis and therefore rebutted any prima facie showing of obviousness. However, the closest prior art utilizing a DEHP plasticized blood collection bag inherently achieved same result, although this fact was unknown in the prior art.).
“The fact that appellant has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious.” Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985) (The prior art taught combustion fluid analyzers which used labyrinth heaters to maintain the samples at a uniform temperature. Although appellant showed that an unexpectedly shorter response time was obtained when a labyrinth heater was employed, the Board held this advantage would flow naturally from following the suggestion of the prior art.). See also Lantech Inc.v. Kaufman Co. of Ohio Inc., 878 F.2d 1446, 12 USPQ2d 1076, 1077 (Fed. Cir. 1989), cert. denied, 493 U.S. 1058 (1990) (unpublished — not citable as precedent) (“The recitation of an additional advantage associated with doing what the prior art suggests does not lend patentability to an otherwise unpatentable invention.”).
Therefore, Applicant’s arguments with respect to claim(s) 1, 3, 5-8 and 15-17 have been fully considered but they are not persuasive.
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/VERA STULII/Primary Examiner, Art Unit 1791