Key points
- The Board, in translation: "[in the proprietor's] opinion, this teaching in example 13, especially in connection with the R99E protease variant, was not a "realistic" starting point (as in point 4.1.2 of T 1379/11) for the task without a retrospective perspective for the person skilled in the art. solution approach, since the focus of document D2 was on other protease variants that were actually examined, in particular the "F49" variant. The expert lacked motivation in the sense of the so-called "could-would approach" to choose example 13 among all 21 examples of document D2 in the light of their entire teaching with a focus on another protease variant, and within example 13 then an R99, and of these to “select” the R99E protease variant mentioned only in claims 2 and 6 as the starting point for the inventive step."
- The Board: "This line of argument is apparently based on a misunderstanding of how the "selection" of the closest prior art is made. It is true that a starting point for determining an inventive step should be realistic in the sense of the criteria developed by the boards of appeal in this context described in point 4.1.2 of T 1379/11. According to these criteria, it should describe an object that serves the same purpose or pursues the same aim, describes a similar use or concerns the same or a similar technical problem, or at least comes from the same or a closely related field as the claimed invention. A second possible criterion is the number of common features. The fact that a teaching could not realistically have been the basis for an invention is not the case, for example, if the teaching comes from an unrelated field that is too distant."
- " The fact that document D2 contains additional examples and describes a number of other protease variants in more detail than the R99E protease variant is therefore irrelevant to the question of whether Example 13 with the R99E protease variant can serve as a starting point for the problem-solution approach. The further, more detailed examples and the alleged focus in document D2 on other protease variants that have actually been examined with regard to their cleaning performance cannot change the technical disclosure of Example 13 and therefore have no influence on the question of whether this is a realistic starting point for the task -solution approach can be."
- "The criteria for selecting a realistic starting point set out in point 4.1.2 of T 1379/11 are met for example 13 of document D2. Document D2, like the patent in suit, provides suitable or improved subtilisin protease variants for use in a detergent or cleaning agent, and all protease variants disclosed in document D2, including those mentioned in Example 13, are intended for this use, as is that in Example 13 liquid cleaning agents described. In this respect, the use of Example 13 as the closest prior art does not constitute a discrepancy with the procedure described in point 4.1.2 of T 1379/11."
- "The difference between the claimed subject matter and the disclosure in Example 13 of document D2 lies in the concentration of the phosphonate. In order to determine the task to be solved, it is necessary to assess whether there is a technical effect associated with this distinguishing feature. This is not the case for the phosphonate concentration range cited in the claim. "
- Example 13 is silent on the concentration of the phosphonate that is used.
- " is therefore no technical effect associated with the difference between the claimed use and the teaching in document D2. Since no concentration for the phosphonate is given in Example 13 of document D2, the problem to be solved can therefore only be seen in the provision of a suitable concentration for the phosphonate in the enzymatic liquid cleaning agent described in Example 13 of document D2."
- The Board: " The use of a HEDP concentration, which falls within the range specified in the claim, was therefore obvious from the teaching in document D2 alone for the person skilled in the art who would like to put example 13 of document D2 into practice."
- " It was therefore obvious to the person skilled in the art to select a concentration for the phosphonate in the liquid cleaning agent described in Example 13 of document D2 from the concentration range specified in the claim. There is therefore no inventive step associated with the subject matter of claim 1 of the main request (Article 100(a) EPC in conjunction with Article 56 EPC).
Main application (patent as granted)
Inventive step (Article 100a) in conjunction with Article 56 EPC) - Claim 1
Closest state of the art
1. Document D2, which, like the contested patent, describes various subtilisin protease variants and their use in detergents and cleaning products, was considered in the contested decision and by both parties in the appeal proceedings to be the most appropriate starting point for assessing inventive step . The Chamber sees no reason to deviate from this assessment. However, the parties disagreed as to whether Example 13 of document D2 was suitable as a starting point in the task-solution approach.
2. Example 13 (see lines 1 to 13 on page 46 of document D2) describes the preparation of a liquid enzymatic cleaning agent by mixing various ingredients at room temperature, including "about 1-hydroxyethane-1,1-diphosphonic acid" (see line 8 of page 46). “A sufficient amount of the protease as defined in claim 6” is then added to this aqueous solution in order to obtain a composition of approximately 0.5% by weight of liquid protease concentrate (see lines 11 to 13 on page 46).
3. Claim 6 of document D2 relates to an enzymatic detergent composition containing a mutated subtilisin protease having one or more of the mutations R99G, R99A, R99S, R99E, L211D, L211E, S154D, S154E. Claim 6 therefore defines, among other things, a mutated R99E subtilisin protease variant. Document D2 also teaches that the mutated subtilisin proteases according to the invention are derived from a specific "Bacillus lentus alkaline protease" ("BLAP" DSM 5483) (see lines 13 to 15 on page 6). The amino acid sequence of this BLAP described on page 6 falls within the amino acid sequence defined in claim 1. Such a mutant BLAP "DSM 5483" protease containing the R99E or R99D mutation is also explicitly disclosed in claim 2 of document D2.
4. Document D2 therefore teaches in Example 13 with reference to claim 6 and in combination with the general teaching on page 6 the use of a subtilisin protease variant comprising an amino acid sequence corresponding to the amino acid sequence specified in SEQ ID NO:1 of the contested patent is at least 80% identical and contains an R99E mutation, in a liquid detergent or cleaning agent that contains the phosphonate 1-hydroxyethane-1,1-diphosphonic acid (hereinafter "HEDP") in an unknown concentration.
5. Contrary to the respondent's opinion, multiple selection of firstly example 13 from all examples in document D2 and secondly the protease variant from the list of claim 6 is not necessary in order to arrive at this teaching. This is the case simply because the reference to the protease variants of claim 6 is within Example 13 and is therefore part of Example 13. It is therefore only necessary to select the R99E protease variant from claim 6 for the teaching of document D2 summarized in point 4 above. Document D2 thus discloses the liquid cleaning agent described in Example 13 containing a protease with at least one of the mutations listed in claim 6, including the R99E mutation.
6. In the respondent's opinion, this teaching in example 13, especially in connection with the R99E protease variant, was not a "realistic" starting point (as in point 4.1.2 of T 1379/11) for the task without a retrospective perspective for the person skilled in the art. solution approach, since the focus of document D2 was on other protease variants that were actually examined, in particular the "F49" variant. The expert lacked motivation in the sense of the so-called "could-would approach" to choose example 13 among all 21 examples of document D2 in the light of their entire teaching with a focus on another protease variant, and within example 13 then an R99, and of these to “select” the R99E protease variant mentioned only in claims 2 and 6 as the starting point for the inventive step.
7. This line of argument is apparently based on a misunderstanding of how the "selection" of the closest prior art is made. It is true that a starting point for determining an inventive step should be realistic in the sense of the criteria developed by the boards of appeal in this context described in point 4.1.2 of T 1379/11. According to these criteria, it should describe an object that serves the same purpose or pursues the same aim, describes a similar use or concerns the same or a similar technical problem, or at least comes from the same or a closely related field as the claimed invention. A second possible criterion is the number of common features. The fact that a teaching could not realistically have been the basis for an invention is not the case, for example, if the teaching comes from an unrelated field that is too distant.
8. On the other hand, the so-called "could-would approach" or the motivation of the expert for the "selection" (ie determination) of the closest state of the art plays no role. Instead, this is done according to the objective criteria mentioned in point 7.
9. The fact that document D2 contains additional examples and describes a number of other protease variants in more detail than the R99E protease variant is therefore irrelevant to the question of whether Example 13 with the R99E protease variant can serve as a starting point for the problem-solution approach. The further, more detailed examples and the alleged focus in document D2 on other protease variants that have actually been examined with regard to their cleaning performance cannot change the technical disclosure of Example 13 and therefore have no influence on the question of whether this is a realistic starting point for the task -solution approach can be.
10. The criteria for selecting a realistic starting point set out in point 4.1.2 of T 1379/11 are met for example 13 of document D2. Document D2, like the patent in suit, provides suitable or improved subtilisin protease variants for use in a detergent or cleaning agent, and all protease variants disclosed in document D2, including those mentioned in Example 13, are intended for this use, as is that in Example 13 liquid cleaning agents described. In this respect, the use of Example 13 as the closest prior art does not constitute a discrepancy with the procedure described in point 4.1.2 of T 1379/11.
11. The Respondent also argues that Example 13 is only a prophetic, unworkable and erroneous example and therefore does not represent a realistic starting point for the task solution approach for these reasons. In particular, due to the lack of HEDP concentration information, it is questionable whether the cleaning agent even contains a phosphonate.
12. Example 13 describes the preparation of a liquid enzymatic cleaning agent by listing all the components contained and the pH of the solution as determined by measurement (see lines 10 and 11 on page 46 "The pH of the resulting solution is 8.1 (measured as a 10% aqueous solution)"). The list of all components and the measurement of the pH value described make it clear that Example 13 is not a prophetic, ie not carried out, example.
13. However, it must be admitted that Example 13 is incorrect, among other things because in the formulation "about 1-hydroxyethane-1,1-diphosphonic acid" (see line 8 on page 46) the concentration information for the phosphonate HEDP is missing.
14. Because the concentration of the phosphonate is not stated, it is not questionable whether the composition taught contains phosphonate at all. It may be that elsewhere in document D2 phosphonates are taught as optional components of a cleaning agent (see the paragraph bridging pages 20 and 21) and are not included in another preferred embodiment (see the paragraph bridging pages 24 and 25 bridged). However, this has no influence on the technical disclosure of Example 13, in which the phosphonate HEDP is explicitly stated as a component of the liquid cleaning agent specified and is therefore present in the liquid cleaning agent described, albeit without any concentration information. Since all other components of the liquid cleaning agent are listed with an indication of their respective concentration, the specialist only needs to add the concentration of a single component to produce the cleaning agent described. The lack of HEDP concentration therefore does not mean that Example 13 cannot be carried out.
15. Another, also obvious, error in Example 13 is that the ingredients citric acid and ethanol are listed twice in the description of the preparation of the liquid detergent (see lines 2 to 9 on page 46: "A liquid enzymatic detergent composition is prepared by mixing together at room temperature about 13 wt% C10-C13 linear alkylbenzene-sulfonic acid, about 5 wt% alkylpolyglycoside(C12-C14), ... about 1 wt% citric acid, about 7 wt% ethanol, about 1 wt% citric acid about 7 wt% ethanol, about 1-hydroxyethane-1,1-diphosphonic acid and the remainder being water").
16. Both components are therefore listed twice one after the other with the same concentration information in a longer list of individual components. The expert immediately recognizes that the double, identical list of components in a composition is factually incorrect and must be corrected by deleting one of the identical entries. Example 13 is therefore understood by the person skilled in the art to mean that the components citric acid and ethanol are only contained once in the composition described in the specified concentration. The incorrect statement of these two components does not lead to the person skilled in the art doubting the presence of the phosphonate HEDP in the liquid cleaning agent described, nor to the fact that Example 13 cannot be carried out.
17. The fact that the R99E protease variant is only mentioned in claims 2 and 6, but not in the description, and that the amino acid sequence of the proteases is not disclosed in claim 6, is also not suitable for the disclosure of the R99E protease variant in document D2 as such to be called into question. As already explained under point 3 above, document D2 on page 6 teaches which subtilisin protease (BLAP DSM 5483) all the variants described are derived from. The R99E protease variant of BLAP DSM 5483 is also described in claim 2 of document D2. The absence of the sequence in claim 6 is therefore not relevant since the technical disclosure of document D2 is considered as a whole to establish the teaching of Example 13.
18. The respondent also points out that there were almost 15 years between the publication of document D2 and the filing date of the patent, without the R99E protease variant having been used in the prior art, and that document D4, which summarizes the findings from D2 Don't mention R99E mutation. This would indicate that the R99E protease variant in document D2 was considered not to have been disclosed by the expert and that its selection by the expert would therefore only have been made retrospectively.
19. These arguments are also unconvincing. The age of a prior publication may, under certain circumstances, provide an indication of the existence of an inventive step, but is not a reason to exclude a priori publication as a suitable starting point for determining inventive step. Document D4 also describes on page 4 that L211D and L211E protease variants can be used in the invention disclosed in document D4 and then refers to document D2 for the production of these L211 protease variants. The reference to document D2 in document D4 therefore gives no indication as to how the technical disclosure of document D2 would have been understood by the person skilled in the art with regard to other protease variants disclosed therein.
20. None of the arguments put forward by the respondent as to why document D2 does not teach the use of an R99E-BLAP protease variant in a liquid detergent or cleaning agent containing phosphonates, despite the explicit disclosure in Example 13, is therefore convincing. Example 13 of document D2 is therefore the closest prior art.
Task to be solved
21. The difference between the claimed subject matter and the disclosure in Example 13 of document D2 lies in the concentration of the phosphonate. In order to determine the task to be solved, it is necessary to assess whether there is a technical effect associated with this distinguishing feature. This is not the case for the phosphonate concentration range cited in the claim. In particular, neither an increased storage stability mentioned by the opposition division nor an additional increased cleaning performance claimed by the respondent can be recognized as a technical effect associated with the phosphonate concentration range mentioned in the claim.
22. Both technical effects are mentioned in the patent. However, these effects were believed to be associated with one of the seven R99 protease variants described in the patent in combination with a phosphonate at any concentration (see paragraph [0008] of the patent). Accordingly, in the examples, the cleaning performance and storage stability of the R99E protease variant were compared with those of two different proteases described in the prior art, a phosphonate (Dequest® 2066, ie DTPMP) in a concentration (0.5% by weight). liquid detergent containing liquid compared (see Examples 1 and 3, Tables 2 and 4 and paragraphs [0128] and [0135] of the patent). Likewise, the cleaning performance of the R99E protease variant was compared with that of a protease described in the prior art in the same liquid dishwashing detergent containing a phosphonate (HEDP) in a concentration (2.4% by weight) (see Example 2, Table 3 and paragraphs [0132] of the patent).
23. However, these experimental data from the patent do not allow any statement to be made about a technical effect associated with a phosphonate concentration of 0.01 to 4% by weight, since no protease-containing detergents or cleaning agents that contain a phosphonate in concentrations within and contained outside the claimed range.
24. In the proceedings before the Opposition Division, the respondent submitted documents D7 and D7a as further experimental evidence for the above-mentioned technical effects, and in the proceedings before the Board of Appeal, document D11.
25. Document D7 compares the cleaning performance after storage of the R99E protease variant with the unmutated wild-type BLAP protease in liquid detergents containing either 0.40 or 2.40 wt% HEDP or DTPMP. For the same reasons as the experiments in the patent specification, these comparisons are not suitable for proving a technical effect for the distinguishing feature. The comparison with the wild-type protease is irrelevant; The phosphonate concentrations examined are all within the range of 0.01 to 4% by weight stated in the claim.
26. Document D7a compares the storage stability of the R99E protease in the absence and presence of the phosphonate DTPMP (0.4 or 2.4 wt%). These data show that the storage stability of the R99E protease variant is increased in a concentration-dependent manner in the presence of DTPMP at both tested concentrations compared to a liquid detergent that does not contain phosphonate. However, as the complainant asserted, the claim is neither limited to the phosphonate DTPMP, nor are the two concentrations tested suitable for the entire concentration range specified in the claim, the lower end of which is only 0.01% by weight and thus by the factor 40 is lower than the lowest tested concentration of 0.4% by weight to provide sufficient coverage. The data in document D7a therefore does not demonstrate a technical effect across the entire breadth of the claim.
27. Document D11, filed in the appeal, shows experiments comparing the cleaning performance of liquid detergents with and without HEDP and DTPMP at two concentrations (0.4 or 2.4% by weight) in the presence of either the wild-type BLAP protease or one which compares R99E, R99D or R99S protease variants. According to the respondent, document D11 is intended to prove that the R99E and R99D protease variants have an increased cleaning performance compared to the wild-type BLAP and the R99S protease variant in the presence of a phosphonate (table under Section 3. "Contribution of enzymes to the cleaning performance of the detergent" ) and increased storage stability (table under Section 4. “Contribution of enzymes to cleaning performance after storage of the detergent”).
28. However, it also applies to these experiments that the comparison with another protease is not relevant for determining a technical effect, since document D2 already discloses a liquid detergent or cleaning agent containing the R99E protease variant and a phosphonate. Relevant are therefore only comparisons of liquid detergents or cleaning agents that contain a protease variant as defined in the claim and a phosphonate in a concentration within the range defined in the claim, and liquid detergents or cleaning agents that contain this protease variant and the phosphonate in a concentration outside of the area defined in the claim.
29. In this regard, document D11 contains data on the cleaning performance and storage stability of liquid detergents containing the R99E or the R99D protease variant and either no phosphonate or DTPMP or HEDP, each at a concentration of either 0.4% by weight or 2, Contain 4% by weight. In these experiments too, the concentration range tested does not cover the entire range defined in the claim, in particular not concentrations close to the respective end points.
30. In addition, the table in section 3 of document D11 shows that for the R99E protease variant not for all phosphonate concentrations tested, namely not for 0.4% by weight of HEDP and not for 2.4% by weight of DTPMP , improved cleaning performance was achieved compared to a liquid detergent that does not contain phosphonate. The table in Section 4 shows that the R99E protease variant examined in this example does not have improved storage stability for all phosphonate concentrations tested, namely not for 2.4% by weight of DTPMP, compared to a liquid detergent that does not Contains phosphonate. Therefore, neither improved cleaning performance nor improved storage stability are shown for the entire claimed width.
31. There is therefore no technical effect associated with the difference between the claimed use and the teaching in document D2. Since no concentration for the phosphonate is given in Example 13 of document D2, the problem to be solved can therefore only be seen in the provision of a suitable concentration for the phosphonate in the enzymatic liquid cleaning agent described in Example 13 of document D2.
Obviousness of the claimed solution
32. In order to solve the task and to put Example 13 of document D2 into practice, the person skilled in the art would choose a phosphonate concentration that is common in the prior art for washing and cleaning solutions. Document D2 itself teaches in lines 10 to 12 on page 21 that the cleaning agents according to the invention contain up to 5% by weight, in particular 0.1 to 2% by weight, of heavy metal complexing agents, in particular aminoalkylene phosphonates, and therefore teaches a concentration that falls within the phosphonate concentration range stated in the claim. The use of a HEDP concentration, which falls within the range specified in the claim, was therefore obvious from the teaching in document D2 alone for the person skilled in the art who would like to put example 13 of document D2 into practice.
33. The respondent argued in this regard that the concentration information on page 21 of document D2 was generic for complexing agents for heavy metals, for which four classes of substances were given as examples, but HEDP was not among them, and it was not clear from document D2 that HEDP was a complexing agent at all be.
34. This argument cannot be followed since the phosphonate HEDP was well known to those skilled in the art as a complexing agent and component of detergents and cleaning agents. This is evidenced, for example, by document D3, a relevant manual (first paragraph on page 4).
35. Document D4 also describes that phosphonates, including the phosphonate HEDP, are preferred complexing agents in liquid detergents or cleaning agents and are used in amounts of 0.01 to 1.5% by weight (see the first full paragraph on page 23 ). When searching for a suitable concentration for the phosphonate in the liquid cleaning agent described in Example 13 of document D2, the person skilled in the art would therefore also have been advised by document D4 of HEDP concentrations that fall within the scope of claim 1. Therefore, the claimed subject matter was also evident from the combination of the teaching in document D2 with the teaching in document D4.
36. The respondent's line of argument that the expert did not combine document D2 with document D4, since the protease mutations R99E and R99D are explicitly not mentioned in document D4, although reference is made to document D2, cannot be followed. As stated above (see point 4), document D2 already discloses a liquid cleaning agent containing the R99E subtilisin protease variant and the phosphonate HEDP, so the skilled person only needs to provide a suitable HEDP concentration in this cleaning agent. Since document D4 also discloses liquid detergents or cleaning agents containing proteases and phosphonates and therefore comes from the same technical area as document D2, to which it even explicitly refers, the person skilled in the art would have combined the teaching in documents D2 and D4 without a retrospective approach.
37. It was therefore obvious to the person skilled in the art to select a concentration for the phosphonate in the liquid cleaning agent described in Example 13 of document D2 from the concentration range specified in the claim. There is therefore no inventive step associated with the subject matter of claim 1 of the main request (Article 100(a) EPC in conjunction with Article 56 EPC).
No comments:
Post a Comment
Do not use hyperlinks in comment text or user name. Comments are welcome, even though they are strictly moderated (no politics). Moderation can take some time.