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WO2017167847A1 - Production de lait à faible teneur en lactose - Google Patents

Production de lait à faible teneur en lactose Download PDF

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Publication number
WO2017167847A1
WO2017167847A1 PCT/EP2017/057488 EP2017057488W WO2017167847A1 WO 2017167847 A1 WO2017167847 A1 WO 2017167847A1 EP 2017057488 W EP2017057488 W EP 2017057488W WO 2017167847 A1 WO2017167847 A1 WO 2017167847A1
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WO
WIPO (PCT)
Prior art keywords
milk
seq
lactose
lactase activity
sequence
Prior art date
Application number
PCT/EP2017/057488
Other languages
English (en)
Inventor
Petrus Jacobus Theodorus Dekker
Cornelis Marinus Muijlwijk
Marten Aalt PAASMAN
Original Assignee
Dsm Ip Assets B.V.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Dsm Ip Assets B.V. filed Critical Dsm Ip Assets B.V.
Priority to EP17714717.0A priority Critical patent/EP3435770A1/fr
Publication of WO2017167847A1 publication Critical patent/WO2017167847A1/fr

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01108—Lactase (3.2.1.108)
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
    • A23C9/00—Milk preparations; Milk powder or milk powder preparations
    • A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
    • A23C9/1203—Addition of, or treatment with, enzymes or microorganisms other than lactobacteriaceae
    • A23C9/1206—Lactose hydrolysing enzymes, e.g. lactase, beta-galactosidase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
    • A23C2220/00—Biochemical treatment
    • A23C2220/10—Enzymatic treatment

Definitions

  • the invention relates to a milk obtainable by a process in which a milk comprising lactose is treated with an enzyme composition comprising lactase activity.
  • the invention also relates to the process itself and to use of an enzyme composition comprising lactase activity in the production of a milk with a low lactose content.
  • Lactose intolerance is perhaps the best-known food sensitivity in the United States and other parts of the world. It is estimated that about 70% of the world's population has a genetically controlled limited ability to digest lactose. Accordingly, there is a growing demand for dairy food products that contain no or only low levels of lactose.
  • Lactase is used commercially to break down lactose in milk to produce dairy products which are suitable for people with lactose intolerance and/or have a sweeter taste. Because glucose and galactose are sweeter than lactose, lactase produces a more pleasant taste. Lactase is also used in the manufacture of ice cream. Lactose crystallizes at the low temperatures of ice cream, whereas glucose and galactose stay liquid and contribute to a smoother texture. Lactase is also used in the conversion of whey into syrup and for the production of condensed milk.
  • the present invention relates to a milk, to a process for production of such a milk and to the use of a lactase composition in a process for the production of a milk having low lactose.
  • the milk may have a low level of lactose (in view of the use of the lactase, i.e. low lactose lactase-treated milk).
  • a milk comprising about 50 mg/L or less lactose obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 or SEQ ID NO: 2, a truncated version of either thereof or a sequence having at least about 60% sequence identity to any thereto.
  • the invention also provides:
  • a milk comprising about 50 mg/L or less lactose obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having lactase activity which is derived from Bifidobacterium bifidum; a process for the production of a milk comprising about 50 mg/L or less lactose, which process comprises:
  • lactase activity is provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 or SEQ ID NO: 2, a truncated version of either thereof or a sequence having at least about 60% sequence identity to any thereto; a process for the production of a milk comprising about 50 mg/L or less lactose, which process comprises:
  • lactase activity is provided by a polypeptide having lactase activity which is derived from Bifidobacterium bifidum a milk comprising about 50 mg/L or less lactose obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 or SEQ ID NO: 2, a truncated version of either thereof or a sequence having at least about 60% sequence identity to any thereto; a milk comprising about 50 mg/L or less lactose obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having lactase activity which is derived from Bifidobacterium bifidum; a process for the production of a milk comprising about 50 mg/L or less lactose which comprises:
  • lactase activity is provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 or SEQ ID NO: 2, a truncated version of either thereof or a sequence having at least about 60% sequence identity to any thereto; a process for the production of a milk comprising about 50 mg/L or less lactose which comprises:
  • lactase activity is provided by a polypeptide having lactase activity which is derived from Bifidobacterium bifidum; use of an enzyme having lactase activity in the production of milk with a low lactose content, which milk is obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 or SEQ ID NO: 2, a truncated version of either thereof or a sequence having at least about 60% sequence identity to any thereto; use of an enzyme having lactase activity in the production of milk with a low lactose content, which milk is obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having lactase activity which is derived from Bifidobacterium bifidum; use of an enzyme having lactase activity in the production of milk with a low lactose content, which milk is obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 or SEQ ID NO: 2, a truncated version of either thereof or a sequence having at least about 60% sequence identity to any thereto; and use of an enzyme having lactase activity in the production of milk with a low lactose content, which milk is obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having lactase activity which is derived from Bifidobacterium bifidum.
  • SEQ ID NOs: 1 and 2 set out the polypeptide sequences of lactase enzymes from Bifidobacterium bifidum.
  • SEQ ID NO: 1 may also be defined with reference to SEQ ID NO: 2 in WO01/90317.
  • SEQ ID NO: 2 may also be defined with reference to the Bbg3 sequence described in Goulas T.K., Goulas A.K., Tzortzis G., Gibson G.R., Appl. Microbiol. Biotechnol. 76(6), 1365 and 1372 (2007).
  • SEQ ID NO: 3 a C-terminal truncation variant, may also be defined with reference to SEQ ID NO: 2 as described in WO2009/071539.
  • SEQ ID NO: 4 another C-terminal truncation variant, may also be defined with reference to SEQ ID NO: 2 as described in WO2014/184189.
  • the articles “a” and “an” are used herein to refer to one or to more than one (i.e. to one or at least one) of the grammatical object of the article.
  • an element may mean one element or more than one element.
  • the invention provides a milk comprising about 50 mg/L or less lactose. The inventors of the present patent application were surprised that a (lactase-treated) milk with such low levels of lactose could be produced/obtained, the invention thus provides a low lactose, lactase-treated milk.
  • the invention concerns a milk comprising about 50 mg/L or less lactose obtainable by a process which comprises:
  • the invention also concerns a milk comprising about 50 mg/L or less lactose obtainable by a process which comprises:
  • At least a part of the lactase activity in the enzyme composition may be provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 or SEQ ID NO: 2, a truncated version of either thereof or a sequence having at least about 60% sequence identity to any thereto.
  • Reference to a truncated version refers to a C-terminal truncated version.
  • At least a part of the lactase activity in the enzyme composition may be provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 or SEQ I D NO: 2 or SEQ ID NO: 3 or SEQ ID NO: 4 or a sequence having at least about 60% sequence identity to any thereto
  • at least a part of the lactase activity is provided by a polypeptide having lactase activity which is derived from Bifidobacterium bifidum.
  • a substance e.g., a nucleic acid molecule or polypeptide
  • derived from a microorganism preferably means that the substance is native to that microorganism or is a variant based on a substance native to the microorganism (for example a truncated version of a polypeptide derived from the microorganism and/or a version which contains one or more substitutions as compared to a polypeptide derived from the microorganism).
  • polypeptide set out in SEQ ID NO: 1 or SEQ ID NO: 2 of the invention is a full-length wild-type sequence of a lactase from Bifidobacterium bifidum.
  • a polypeptide having lactase activity suitable for use in the invention may comprise an amino acid sequence having at least about 60%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about, 86%, at least about 87%, at least about 88%, at least about 89%, at least about 90%, at least about 91 %, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98% or at least about 99% sequence identity to SEQ ID NO: 1 or SEQ ID NO: 2.
  • SEQ ID NO: 1 and 2 both comprise a signal sequence which is positioned at amino acids 1 to 32 for both of them.
  • a polypeptide having lactase activity for use in the invention preferably comprises:
  • amino acid sequence having at least about 60%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about, 86%, at least about 87%, at least about 88%, at least about 89%, at least about 90%, at least about 91 %, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98% or at least about 99% sequence identity to amino acids 33 to 1752 of SEQ ID NO: 1 .
  • amino acid sequence having at least about 60%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about, 86%, at least about 87%, at least about 88%, at least about 89%, at least about 90%, at least about 91 %, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98% or at least about 99% sequence identity to amino acids 33 to 1935 of SEQ ID NO: 2.
  • a truncated version of the polypeptide of SEQ ID NO: 1 or SEQ ID NO: 2, or more preferably a truncated version of amino acids 33 to 1752 of SEQ ID NO: 1 or a truncated version of amino acids 33 to 1935 of SEQ ID NO:2, may be used or a polypeptide comprising an amino acid sequence having at least about 60%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about, 86%, at least about 87%, at least about 88%, at least about 89%, at least about 90%, at least about 91 %, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98% or at least about 99% sequence identity to such a truncated version of SEQ ID NO: 1 or SEQ ID NO: 2 or more preferred to a truncated version of amino acids 33 to 1752 of SEQ ID NO:
  • polypeptide having lactase activity suitable for use in the invention is the Bbg3 polypeptide described in Goulas T.K., Goulas A.K., Tzortzis G., Gibson G.R., Appl. Microbiol. Biotechnol. 76(6), 1365 and 1372 (2007).
  • Suitable truncated versions of the polypeptide of SEQ ID NO: 1 or SEQ ID NO: 2 include SEQ ID NO: 2 in WO2009/071539 (herein SEQ ID NO: 3) and SEQ ID NOs: 1 or 2 in WO2014/184189 (SEQ ID NO: 2 of WO2014/184189 is SEQ ID NO: 4 in this patent application).
  • the invention provides a milk or a process according to the invention in which SEQ ID NO: 3 or 4 is used or a polypeptide comprising an amino acid sequence having at least about 60%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about, 86%, at least about 87%, at least about 88%, at least about 89%, at least about 90%, at least about 91 %, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98% or at least about 99% sequence identity to SEQ ID NO: 3 or SEQ ID NO: 4.
  • SEQ ID NO: 3 and 4 both comprise a signal sequence which is positioned at amino acids 1 to 27 for both of them.
  • a polypeptide having lactase activity for use in the invention preferably comprises:
  • amino acid sequence having at least about 60%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about, 86%, at least about 87%, at least about 88%, at least about 89%, at least about 90%, at least about 91 %, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98% or at least about 99% sequence identity to amino acids 28 to 1341 of SEQ I D NO: 3, more preferably amino acids 28-1331 of SEQ ID NO: 3 (as amino acids 1332-1341 comprise a purification tag which is preferably removed)
  • amino acid sequence having at least about 60%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about, 86%, at least about 87%, at least about 88%, at least about 89%, at least about 90%, at least about 91 %, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98% or at least about 99% sequence identity to amino acids 28 to 1331 of SEQ ID NO: 4.
  • the invention concerns a milk comprising about 50 mg/L or less lactose obtainable by a process which comprises:
  • the invention also concerns a milk comprising about 50 mg/L or less lactose obtainable by a process which comprises:
  • lactase activity is provided by a polypeptide having an amino acid sequence which comprises the sequence set out in SEQ ID NO: 1 , 2, 3 or 4 or a sequence having at least 60% sequence identity to SEQ ID NO: 1 , 2, 3 or 4.
  • At least part of the lactase activity is provided by a polypeptide having an amino acid sequence which comprises the sequence set out in amino acids 33 to 1752 of SEQ ID NO: 1 , amino acids 33 to 1935 of SEQ I D NO: 2, amino acids 28 to 1331 of SEQ ID NO:3 or amino acids 28 to 1331 of SEQ ID NO: 4 or a sequence having at least 60% sequence identity to any thereto.
  • a low temperature batch process is one which is typically carried out a temperature of from about 5°C to about 10°C, for example at about 6°C to about 9°C.
  • the enzyme composition comprising lactase activity may be used so that from about 2000 to about 5000 NLU/L lactase activity is provided. More preferably, the skilled person determines the suitable amount of enzyme based on the specific enzyme characteristics. The skilled person is very well capable of determining the suitable amount of enzyme needed to achieve the desired degree of lactose hydrolysis. The enzyme activity may also be expressed in a different unit, for example in LAU.
  • the used incubation time depends on the amount of NLU/L milk and is typically in the range of 20 to 48 hours.
  • the low temperature batch process is performed at from about 5°C to about 10°C and incubation is performed from about 20 to about 48 hours.
  • An aseptic process is one which is typically carried out at ambient temperature, for example a temperature of at least about 20°C, for example at least about 25°C.
  • the enzyme composition comprising lactase activity may be used so that from about 200 to about 500 NLU/L lactase activity is provided.
  • An aseptic process may be the FlexDosTM or Aldose systems.
  • An aseptic process is a process in which milk is first pasteurized or sterilized and cooled to ambient temperature, at which time sterile filtered lactase is added and the product sterile packed. The lactase is allowed to react with lactose in the milk over several days.
  • An example of a resulting milk is low lactose UHT milk.
  • the invention provides a milk obtainable by the process of the invention.
  • milk is intended to encompass milks from mammals and plant sources or mixtures thereof.
  • the milk is from a mammal source.
  • Mammals sources of milk include, but are not limited to cow, sheep, goat, buffalo, camel, llama, mare and deer.
  • the milk is from a mammal selected from the group consisting of cow, sheep, goat, buffalo, camel, llama, mare and deer, and combinations thereof.
  • Plant sources of milk include, but are not limited to, milk extracted from soy bean, pea, peanut, barley, rice, oat, quinoa, almond, cashew, coconut, hazelnut, hemp, sesame seed and sunflower seed. Soy bean milk is preferred.
  • milk refers to not only whole milk, but also skim milk or any liquid component derived thereof.
  • low lactose milk refers to a milk which comprises about 50mg/L or less lactose, about 40mg/L or less lactose, about 30mg/L or less lactose, about 20mg/L or less lactose or about 10mg/L or less lactose. Such concentrations may be reached in about 48 hours or less, about 32 hours or less or about 24 hours or less (when a milk is treated as described herein).
  • the milk could be a pasteurized milk, a UHT-milk or milk reconstituted from all or part of its original constituents with or without intermediate processing steps such as protein hydrolysis.
  • Treatment with an enzyme composition comprising lactase activity may be done prior to and after the heat-treatment of the milk.
  • the lactase treatment may be done by adding the enzyme to the milk.
  • the invention also provides:
  • the enzyme composition comprising lactase activity may be as described herein.
  • milk with a low lactose content refers to a milk which comprises about 50mg/L or less lactose, about 40mg/L or less lactose, about 30mg/L or less lactose, about 20mg/L or less lactose or about 10mg/L or less lactose.
  • sequence homology or “sequence identity” or “homology” or “identity” are used interchangeably herein.
  • sequences are aligned for optimal comparison purposes.
  • gaps may be introduced in any of the two sequences that are compared.
  • alignment can be carried out over the full length of the sequences being compared.
  • the alignment may be carried out over a shorter length, for example over about 20, about 50, about 100 or more nucleic acids/based or amino acids.
  • sequence identity is the percentage of identical matches between the two sequences over the reported aligned region.
  • a comparison of sequences and determination of percentage of sequence identity between two sequences can be accomplished using a mathematical algorithm.
  • the skilled person will be aware of the fact that several different computer programs are available to align two sequences and determine the identity between two sequences (Kruskal, J. B. (1983) An overview of sequence comparison In D. Sankoff and J. B. Kruskal, (ed.), Time warps, string edits and macromolecules: the theory and practice of sequence comparison, pp. 1 -44 Addison Wesley).
  • the percent sequence identity between two amino acid sequences or between two nucleotide sequences may be determined using the Needleman and Wunsch algorithm for the alignment of two sequences. (Needleman, S. B. and Wunsch, C. D. (1970) J. Mol. Biol.
  • the percentage of sequence identity between a query sequence and a sequence of the invention is calculated as follows: Number of corresponding positions in the alignment showing an identical amino acid or identical nucleotide in both sequences divided by the total length of the alignment after subtraction of the total number of gaps in the alignment.
  • the identity defined as herein can be obtained from NEEDLE by using the NOBRIEF option and is labeled in the output of the program as "longest-identity".
  • nucleic acid and protein sequences of the present invention can further be used as a "query sequence" to perform a search against public databases to, for example, identify other family members or related sequences.
  • search can be performed using the NBLAST and XBLAST programs (version 2.0) of Altschul, et al. (1990) J. Mol. Biol. 215:403—10.
  • Gapped BLAST can be utilized as described in Altschul et al., (1997) Nucleic Acids Res. 25(17): 3389-3402.
  • the default parameters of the respective programs e.g., XBLAST and NBLAST
  • Lactase enzymes were expressed in Bacillus subtilis for comparison with Maxilact LGI (DSM Food Specialties, Delft, NL).
  • Lad 6 is described in WO2009/071538 (SEQ ID NO: 2; herein SEQ ID NO: 3) and Iac19 (herein SEQ ID NO: 2) is described as Bbg3 in Goulas T.K., Goulas A.K., Tzortzis G., Gibson G.R., Appl. Microbiol. Biotechnol. 76(6), 1365 and 1372 (2007).
  • Standard genetic techniques such as overexpression of enzymes in the host cells, genetic modification of host cells, or hybridisation techniques, are known methods in the art, such as described in Sambrook and Russel (2001 ) "Molecular Cloning: A Laboratory Manual (3 rd edition), Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, or F. Ausubel et al, eds., "Current protocols in molecular biology", Green Publishing and Wiley Interscience, New York (1987). Methods for transformation, genetic modification etc of fungal host cells are known from e.g.
  • Enzymes were isolated from the fermentation broth of Bacillus subtilis strains and purified using standard centrifugation and filtration techniques.
  • Example 1 application of the lactase enzymes in the milk pre-sterilization process (6°C)
  • Substrate "Halfvolle melk from Jumbo supermarket”. For each enzyme 2 vials each containing 18.4 ml of semi-skimmed pasteurized and homogenized milk was equilibrated at 6°C before start of the experiment. Lactase was dosed based on the amount of specific protein at 20 mg/l milk in duplicate and incubation is continued at 6°C.
  • the different Bifidobacterium lactases were tested for activity in pasteurized milk by incubation at 6°C and taking samples at various time points, as described above.
  • This method represents the batch process (also called pre-sterilization process).
  • the different Bifidobacterium lactases were dosed in UHT milk and incubated at 25°C, representing the aseptic process (also called post-sterilization process). Dosage of all lactases was based on the protein giving however the most fair comparison between the Bifidobacterium lactases and Maxilact.

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Abstract

L'invention concerne un lait pouvant être obtenu par un procédé comprenant : a) la fourniture d'un lait contenant du lactose; et b) le traitement dudit lait dans un procédé discontinu à basse température ou un procédé aseptique avec une composition enzymatique comprenant une activité de la lactase, au moins une partie de l'activité de la lactase étant fournie par un polypeptide ayant une séquence d'acides aminés qui comprend la séquence définie dans SEQ ID NO: 1 OU SEQ ID NO : 2, une version tronquée de l'une ou l'autre desdites séquences ou une séquence ayant au moins environ 60 % d'identité de séquence avec l'une quelconque desdites séquences.
PCT/EP2017/057488 2016-03-31 2017-03-30 Production de lait à faible teneur en lactose WO2017167847A1 (fr)

Priority Applications (1)

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US201662316460P 2016-03-31 2016-03-31
US62/316,460 2016-03-31

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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
BE1026724B1 (nl) * 2018-10-24 2020-05-28 Inex Nv Melkproduct met een verlaagd lactosegehalte en een werkwijze ter vervaardiging van het melkproduct

Citations (13)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1990014423A1 (fr) 1989-05-18 1990-11-29 The Infergene Company Transformation de microorganismes
EP0481008A1 (fr) 1989-07-07 1992-04-22 Unilever Plc Procede de preparation d'une proteine a partir d'un champignon transforme par integration multicopie d'un vecteur d'expression
EP0635574A1 (fr) 1993-07-23 1995-01-25 Gist-Brocades N.V. Souches récombinantes dépourvues de marqueurs de sélection: procédé pour leur obtention et utilisation de ces souches
WO1998046772A2 (fr) 1997-04-11 1998-10-22 Dsm N.V. Transformation genetique comme outil pour la construction de champignons filamenteux industriels de recombinaison
WO1999060102A2 (fr) 1998-05-19 1999-11-25 Dsm N.V. Perfectionnement d'un procede de production de cephalosporines
WO2000037671A2 (fr) 1998-12-22 2000-06-29 Dsm N.V. Production in vivo amelioree de cephalosporines
US6265186B1 (en) 1997-04-11 2001-07-24 Dsm N.V. Yeast cells comprising at least two copies of a desired gene integrated into the chromosomal genome at more than one non-ribosomal RNA encoding domain, particularly with Kluyveromyces
WO2001090317A2 (fr) 2000-05-26 2001-11-29 Arla Foods Amba Nouvelle enzyme isolee a partie de bifidobacterium
WO2009071538A2 (fr) 2007-12-04 2009-06-11 Shell Internationale Research Maatschappij B.V. Procédé et appareil permettant de refroidir et/ou de liquéfier un flux d'hydrocarbure
WO2009071539A1 (fr) 2007-12-03 2009-06-11 Novozymes A/S Procédé de fabrication d'un produit laitier
WO2014184189A2 (fr) 2013-05-14 2014-11-20 Novozymes A/S Procédé de saccharification et de fermentation simultanées de perméat de lactosérum
WO2015086746A1 (fr) * 2013-12-11 2015-06-18 Dupont Nutrition Biosciences Aps Procédé de préparation d'un produit laitier en teneur stable en galacto-oligosaccharide(s)
WO2015132402A1 (fr) * 2014-03-06 2015-09-11 Arla Foods Amba Produits laitiers à teneur réduite en lactose contenant des galacto-oligosaccharides et des monosaccharides et procédé de production

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
NZ702287A (en) * 2012-06-08 2016-06-24 Dupont Nutrition Biosci Aps Polypeptides having transgalactosylating activity

Patent Citations (13)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1990014423A1 (fr) 1989-05-18 1990-11-29 The Infergene Company Transformation de microorganismes
EP0481008A1 (fr) 1989-07-07 1992-04-22 Unilever Plc Procede de preparation d'une proteine a partir d'un champignon transforme par integration multicopie d'un vecteur d'expression
EP0635574A1 (fr) 1993-07-23 1995-01-25 Gist-Brocades N.V. Souches récombinantes dépourvues de marqueurs de sélection: procédé pour leur obtention et utilisation de ces souches
US6265186B1 (en) 1997-04-11 2001-07-24 Dsm N.V. Yeast cells comprising at least two copies of a desired gene integrated into the chromosomal genome at more than one non-ribosomal RNA encoding domain, particularly with Kluyveromyces
WO1998046772A2 (fr) 1997-04-11 1998-10-22 Dsm N.V. Transformation genetique comme outil pour la construction de champignons filamenteux industriels de recombinaison
WO1999060102A2 (fr) 1998-05-19 1999-11-25 Dsm N.V. Perfectionnement d'un procede de production de cephalosporines
WO2000037671A2 (fr) 1998-12-22 2000-06-29 Dsm N.V. Production in vivo amelioree de cephalosporines
WO2001090317A2 (fr) 2000-05-26 2001-11-29 Arla Foods Amba Nouvelle enzyme isolee a partie de bifidobacterium
WO2009071539A1 (fr) 2007-12-03 2009-06-11 Novozymes A/S Procédé de fabrication d'un produit laitier
WO2009071538A2 (fr) 2007-12-04 2009-06-11 Shell Internationale Research Maatschappij B.V. Procédé et appareil permettant de refroidir et/ou de liquéfier un flux d'hydrocarbure
WO2014184189A2 (fr) 2013-05-14 2014-11-20 Novozymes A/S Procédé de saccharification et de fermentation simultanées de perméat de lactosérum
WO2015086746A1 (fr) * 2013-12-11 2015-06-18 Dupont Nutrition Biosciences Aps Procédé de préparation d'un produit laitier en teneur stable en galacto-oligosaccharide(s)
WO2015132402A1 (fr) * 2014-03-06 2015-09-11 Arla Foods Amba Produits laitiers à teneur réduite en lactose contenant des galacto-oligosaccharides et des monosaccharides et procédé de production

Non-Patent Citations (9)

* Cited by examiner, † Cited by third party
Title
"Current protocols in molecular biology", 1987, GREEN PUBLISHING AND WILEY INTERSCIENCE
ALTSCHUL ET AL., J. MOL. BIOL., vol. 215, 1990, pages 403 - 10
ALTSCHUL ET AL., NUCLEIC ACIDS RES., vol. 25, no. 17, 1997, pages 3389 - 3402
GOULAS T.K.; GOULAS A.K.; TZORTZIS G.; GIBSON G.R., APPL. MICROBIOL. BIOTECHNOL., vol. 76, no. 6, 2007, pages 1365,1372
KRUSKAL, J. B.: "Time warps, string edits and macromolecules: the theory and practice of sequence comparison", 1983, ADDISON WESLEY, article "An overview of sequence comparison", pages: 1 - 44
NEEDLEMAN, S. B.; WUNSCH, C. D., J. MOL. BIOL., vol. 48, 1970, pages 443 - 453
PRANATHI PERATI; BRIAN DE BORBA; JEFFREY ROHRER, THERMO FISHER SCIENTIFIC, SUNNYVALE, CA, USA, vol. 248, 2015, pages 1 - 8
RICE,P.; LONGDEN,L.; BLEASBY,A.: "EMBOSS: The European Molecular Biology Open Software Suite", TRENDS IN GENETICS, vol. 16, no. 6, 2000, pages 276 - 277, XP004200114, Retrieved from the Internet <URL:http://emboss.bioinformatics.nl> DOI: doi:10.1016/S0168-9525(00)02024-2
SAMBROOK; RUSSEL: "Molecular Cloning: A Laboratory Manual", 2001, COLD SPRING HARBOR LABORATORY PRESS

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
BE1026724B1 (nl) * 2018-10-24 2020-05-28 Inex Nv Melkproduct met een verlaagd lactosegehalte en een werkwijze ter vervaardiging van het melkproduct

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