Unlock instant, AI-driven research and patent intelligence for your innovation.

Methods for producing lipases

By changing the polynucleotide sequence of lipase to introduce disulfide bonds, reducing the hydrolysis activity and reactivating it under the action of an activator, the problem of insufficient stability and washing performance of existing lipase in harsh environments is solved, achieving a more efficient Lipid stain removal.

Active Publication Date: 2018-08-21
NOVOZYMES AS
View PDF245 Cites 6 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Current cleaning and / or fabric care compositions contain a number of active ingredients that interfere with the ability of lipases to remove lipid stains, and in particular the stability of lipases in such compositions remains a challenge

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0183] Preparation of variants

[0184] The present invention also relates to methods for obtaining lipase variants and / or fragments thereof, these methods comprising introducing into the parent lipase at positions -57, -54, -47, -46,-corresponding to SEQ ID NO: 2 One of 43, -40, -38, -37, -36, -33, -31, -24, 101, 102, 104, 120, 182, 186, 212, 216, 239, 240, 246, and 249 or Substitution at multiple positions, where the variant and / or fragment has lipase activity; and recovering the variant and / or fragment.

[0185] The present invention also relates to methods for obtaining lipase variants and / or fragments thereof. These methods include introducing into the parent lipase at positions corresponding to -57, -54, -47, -46, -43, -40,- 38, -37, -36, -33, -31, and -24 substitutions at one or more positions, and included in positions 101, 102, 104, 120, 182, 186 corresponding to SEQ ID NO: 2 , 212, 216, 239, 240, 246, and 249 at one or more positions.

[0186] In some aspects, the presen...

example

[0614] The following examples include Rhizomucor miehei lipase (RmL) and Thermomyces lanuginosa lipase (TlL) variants. Two such preferred RmL variants are called RPPI0018 (P182C T-40C) and RPPI0019 (N186C P-46C).

[0615] SEQ ID No: 1 lists the nucleotide sequence of RmL, including the sequence encoding the following cleaved prepropeptide (underlined):

[0616]

[0617]

[0618] SEQ ID No: 2 lists the amino acid sequence of RmL, including the following cleaved preprosequence (underlined):

[0619]

[0620] SEQ ID No: 3 lists the amino acid sequence of the RmL mature protein:

[0621]

[0622]

[0623] SEQ ID No: 4 lists the amino acid sequence of the propeptide of RmL:

[0624] VPIKRQSNST VDSLPPLIPS RTSAPSSSPS TTDPEAPAMS RNGPLPSDVE TKYGMALNATSYPDSVVQAM

[0625] SEQ ID No: 5 lists the nucleotide sequence of TlL, including the sequence encoding the following cleaved prepropeptide (underlined):

[0626]

[0627] SEQ ID No: 6 lists the amino acid sequence of TlL, including the following clea...

example 1

[0639] Example 1: Thermal stability

[0640] Using a VP-Capillary Differential Scanning Calorimeter (MicroCal Inc., Piscataway, New Jersey, USA), the RmL wild type together with the RmL variant was determined by differential scanning calorimetry (DSC) The thermal stability of RPPI0018 and RPPI0019. At a constant programmed heating rate of 200K / hr, heating in buffer (50mM HEPES; pH 8.0; 0.2mM CaCl 2 In the thermogram (Cp vs. T) obtained after the enzyme solution in ), the thermal denaturation temperature Td (°C) is regarded as the top of the denaturation peak (main endothermic peak). A similar experiment was run in which 1 mM LAS (anionic surfactant) or 0.05 mg / mL Relase (thermostable protease, Novozymes) was added to the buffer. Load the sample solution and reference solution (approximately 0.2 mL) into the calorimeter (reference solution: buffer without enzyme) from the storage condition of 10°C, and before the DSC scan from 20°C to 100°C, Heat pre-equilibration at 20°C for ab...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The present invention relates to a method for generating a preparation of a lipase variant of a parent lipase comprising a step of altering one or more nucleotides in a polynucleotide encoding the parent lipase, wherein the alteration provides at least one disulfide bond and a hydrolytic activity of said lipase variant which is reduced as compared with the hydrolytic activity of the parent lipase.The invention also relates to a polynucleotide encoding the lipase variant, the lipase variant and its use.

Description

[0001] Reference to Sequence Listing [0002] This application contains a sequence listing in computer readable form, which is incorporated herein by reference. Technical field [0003] The present invention relates to lipase variants, polynucleotides encoding these variants, methods of producing these variants, and methods of using these variants. Background technique [0004] Lipase is an important biocatalyst, which has been shown to be useful for different applications. Lipase has been used to remove lipid stains and has been added to different compositions. Current cleaning and / or fabric care compositions contain many active ingredients that interfere with the ability of lipases to remove lipid stains, and particularly the stability of lipases in such compositions remains a challenge. There is a need for lipases that can function in the harsh environment of compositions for cleaning. Summary of the invention [0005] For many years, lipases have been successfully used in vari...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): C12N9/18
CPCC12Y301/01003C12N9/20C11D3/38627
Owner NOVOZYMES AS