IP Library › Granted Patent US 12,371,726
Granted Patent B2
US 12,371,726 · App. 18/286,782 · Granted Jul 29, 2025

Process to produce mono-rhamnolipids

Inventors: Natalia Eliza Iyke Domeradzka (Liverpool, GB); Dietmar Andreas Lang (Liverpool, GB); Neil James Parry (Tarporley, GB); Mark Lawrence Thompson (Ellesmere Port, GB)
Assignee: Conopco, Inc.
C12P19/44C12P7/6481C12P19/14C11D1/662
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Quick Facts
Patent No.
US 12,371,726
App. No.
18/286,782
Granted
Jul 29, 2025
Kind
B2
Abstract

The invention concerns a process to convert di-rhamnolipid to mono-rhamnolipid, using an α-L-rhamnosidase enzyme which has a sequence identity of at least 70% with either SEQ ID. 1 or SEQ. ID 2.

Claims (20)

1. A process to convert di-rhamnolipid to mono-rhamnolipid comprising, using an α-L-rhamnosidase enzyme which has a sequence identity of at least 70% with either SEQ ID. 1 or SEQ ID. 2;

wherein the process to convert di-rhamnolipid to mono-rhamnolipid comprises:

(a) contacting a starting di-rhamnolipid material with an α-L-rhamnosidase enzyme which is immobilised on a support by covalent bonding; and

(b) separating a produced mono-rhamnolipid from a reaction medium, side products, and a combination thereof.

2. The process according to claim 1 , wherein the α-L-rhamnosidase enzyme has a sequence identity of at least 75% with either SEQ ID. 1 or SEQ ID. 2.

3. The process according to claim 1 , wherein the starting di-rhamnolipid material has a carbon alkyl length of from C8 to C14.

4. The process according to claim 1 , wherein the resulting mono-rhamnolipid material has a carbon alkyl length of from C8 to C14.

5. The process according to claim 1 , wherein a rhamnose by-product is removed from the enzymatic reaction mixture as the reaction progresses.

6. The process according to claim 1 , wherein a temperature during the reaction is from 10 to 60° C.

7. The process according to claim 1 , wherein a pH during the reaction is from pH 5 to 10.

8. The process according to claim 2 , wherein the α-L-rhamnosidase enzyme has a sequence identity of at least 85% with either SEQ ID. 1 or SEQ ID. 2.

9. The process according to claim 2 , wherein the α-L-rhamnosidase enzyme has a sequence identity of at least 95% with either SEQ ID. 1 or SEQ ID. 2.

10. The process according to claim 3 , wherein the starting di-rhamnolipid material has a carbon alkyl length of from C8-C12.

11. The process according to claim 4 , wherein the resulting mono-rhamnolipid material has a carbon alkyl length of from C8-C12.

12. The process according to claim 6 , wherein the temperature during the reaction is from 15 to 50° C.

13. The process according to claim 6 , wherein the temperature during the reaction is from 18 to 45° C.

14. The process according to claim 6 , wherein the temperature during the reaction is from 20 to 45° C.

15. The process according to claim 7 , wherein the pH during the reaction is from pH 5 to 9.

16. The process according to claim 7 , wherein the pH during the reaction is from pH 5.5 to 8.5.

17. The process according to claim 7 , wherein the pH during the reaction is from pH 6 to 8.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 12, 2023
From: DOMERADZKA, NATALIA ELIZA IYKE; LANG, DIETMAR ANDREAS; PARRY, NEIL JAMES; THOMPSON, MARK LAWRENCE
To: CONOPCO, INC., D/B/A UNILEVER
Reel/Frame 065843/0183 →
Priority Claims (1)
EP 21171246 · Apr 29, 2021 · regional
Continuity (1)
Related Publication 20240093257A1 · Mar 21, 2024
References Cited (33)
US 4971812A · Tsen · 1990 [cited by examiner]
US 8658407B2 · Lyons · 2014 [cited by examiner]
US 9243212B2 · Kuppert et al. · 2016 [cited by applicant]
US 10292924B2 · Schilling et al. · 2019 [cited by applicant]
US 10941173B2 · Lu et al. · 2021 [cited by applicant]
US 20170175151A1 · Ju · 2017 [cited by examiner]
US 20180016525A1 · Scheuermann et al. · 2018 [cited by applicant]
CS 257830 · 1988 [cited by examiner]
EP 2786743 · 2014 [cited by applicant]
EP 2787065 · 2014 [cited by applicant]
EP 2596087 · 2015 [cited by applicant]
Bodakowska et al., Molecule 2020, 25, 2731, doi:10.3390/molecules25122731, avaiable on the internet. [cited by examiner]
De Vries et al., UniProt Database, Accession No. AOA1L9UF14, Mar. 2017. [cited by examiner]
Magario et al.; “Evaluation of enzyme carriers as biocatalysts for the conversion of emulsified rhamolipds”; Biocatalysis and Biotransformation; vol. 27; pp. 237-245 (2009). [cited by applicant]
Rathankumar et al.; “Application of statistical modeling for the production of highly pure rhamnolipids using magnetic biocatalysts: Evaluating its efficiency as a bioremedition agent”; Journal of Hazardous Materials; v… [cited by applicant]
Nitschke et al.; “Rhamnolipid Surfactants: An Update on the General Aspects of These Remarkable Biomolecules”; Biotechnology Progress; vol. 21; pp. 1593-1600 (2005). [cited by applicant]
Mohammad et al.; “Rhamnolipids: diversity of structures, microbial origins and roles”; Applied Microbiology and Biotechnology; vol. 86; pp. 1323-1336 (2010). [cited by applicant]
Ahmed et al.; “Methods of Enzyme Immobilzation on Various Supports”; Materials Research Foundations; vol. 44; pp. 1-28 (2019). [cited by applicant]
Wahab et al.; “On the taught new tricks of enzymes immobilization: An all-inclusive overview”; Reactive and Functional Polymers; vol. 152; pp. 1-26 (2020). [cited by applicant]
Gallego et al.; “Purification and Characterization of an α-L Rhamnosidase from Aspergillus terreus of interest in Winemaking”; Food Chemistry and Toxicology; vol. 66; pp. 204-209 (2001). [cited by applicant]
Magario et al.; “Kinetic Analysis and Modeling of the Liquid-Liquid Conversion of Emulsified di-Rhamnolipids by Naringinase From Penicillium decumbens”; Biotechnolgy and Bioenginereing; vol. 9999; pp. 1-11 (2008). [cited by applicant]
Puri; “Updates on naringinase: Structural and biotechnological aspects”; Applied Microbiology and Biotechnology; vol. 93; pp. 49-60 (2011). [cited by applicant]
Muller, et al., “Rhamnolipids—Next generation surfactants?,” Journal of Biotechnology, 162 (2012) pp. 366-380, Elsevier BV. [cited by applicant]
Gerstorferova, et al, “Recombinant a-L-rhamnosidase from Apergillus terreus in selective trimming of rutin,” Process Biochemistry, 47 (2012), pp. 828-835, 47, Elsevier Ltd. [cited by applicant]
Rebros, et al. “Recombinant a-L-rhamnosidase of Apergillus terreus immobilization in polyvinylalcohol hydrogel and its apllication in rutin derhamnosylation,” Biocatalysis and Biotransformation, 2013; 31 (6), pp. 329-33… [cited by applicant]
Krasnan, et al., “Immobilization of cells and enzymes to LentiKats,” Applied Microbiology and Biotechnology (2016) 100: pp. 2535-2553, Springer-Verlag Berlin Heidelberg. [cited by applicant]
International Preliminary Report on Patentability issued in International Application No., PCT/EP2022/060823 dated Nov. 9, 2023. [cited by applicant]
International Search Report and Written Opinion issued in International Patent Application No. PCT/EP2022/060823 dated Sep. 5, 2022. [cited by applicant]
European Search Report and Written Opinion issued in European Patent Application No. EP21171230 dated Nov. 18, 2021. [cited by applicant]
International Search Report and Written Opinion issued in International Patent Application No. PCT/EP2022/060848 dated Aug. 31, 2022. [cited by applicant]
International Preliminary Report on Patentability issued in International Patent Application No. PCT/EP2022/060848 dated Nov. 9, 2023. [cited by applicant]
European Search Report and Written Opinion issued in European Patent Application No. EP21171246 dated Nov. 10, 2021. [cited by applicant]
Gencore, Title “US-18-286-782-1 (Aspergillus terreus alpha-L-rhamnosidase)” GenBank Accession No. JN899401, (2012) pp. 1-3, Biocceleration Ltd. [cited by applicant]