Novo Nordisk A/s

Novozymes A/s

Novo Industri A/s

Martin Schulein

Helle Outtrup

Lene Nonboe Andersen

Markus Sakari Kauppinen

Claus Dambmann

Arne Agerlin Olsen

Henrik Bisgangrd-Frantzen

Kirk Matthew Schnorr

Per Lina Jorgensen

Lene Lange

Claus Von Der Osten

Mads Eskelund Bjornvad

Jack Bech Nielsen

Georg W Jensen

Hans A Olsen

Steen Riisgaard

Shinobu Takagi

Grethe Norskov Rasmussen

Jens L Adler-Nissen

Michiko Ihara

Per Linaa Jorgensen

Peter Rosholm

So Slashedren Lassen

Kirsten Bo Levring

Henrik Gurtler

Carsten Schau Andersen

Kim Vilbour Andersen

Soren Flensted Lassen

Mads E Bjoernvad

Lars Kongsbak

Ruby Ilum Nielsen

Steffen Ernst

Henri Chanzy

Karen Margrethe Oxenbo Slashedll

William Helbert

Egon Nielsen

Torben Henriksen, Legal Representative

Tommy Lykke Husum

Bo Damgaard

Henrik Fredholm

Carsten Mailand Hjorth

Shamkant Anant Patkar

Torben Halkier

Mary Ann Stringer

Wenping Wu

Hans Peter Heldt-Hansen

Henrik Dalbo Slashedge

Sven Hastrup

Torben Peter Frandsen

Mads Eskelund Bj&oslash;rnvad

Lars Saaby Pedersen

Sanne O Schroder Glad

Reinhard Wilting

Carsten Mailand Hjort

Lars Hylling Christensen

Fred Hagen

Hanne Dela, Legal Representative

Masaki Sharyo

Hiromichi Sakaguchi

Per Linang Jo Slashedrgensen

Jan Mo Mikkelsen

Sanne O Schr&oslash;der Glad

Christian Hansen

Annette Hanne Toft

Thomas Vollmond

Neal Franks

Svend Aage Hansen

Lars Christiansen

Iben Angelica Norrevang

Ruby Iium Nielsen

Masahiro Onishi

Per Lina J&oslash;rgensen

Merete Fich

Torben Peter

Charlotte Schou

Jens L Alder-Nissen

Henrick Gurtler

Niels Erik Lange

Mamoru Takahashi

Masahiro Ohishi

Hitoshi Tamagawa

Katsunori Kida

Mads Eskelund Bjo Slashedrnvad

The present invention relates to enzyme preparations consisting essentially of an enzyme which has cellulytic activity, which perform very well in industrial applications such as laundry compositions, for biopolishing of newly manufactured textiles, for providing an abraded look of cellulosic fabric or garment, and for treatment of paper pulp. Further, the invention relates to DNA constructs encoding such enzymes, a method for providing a gene encoding for such enzymes, a method of producing the enzymes, enzyme preparations containing such enzymes, and the use of these enzymes for a number of industrial applications.

Method of providing color clarification of laundry

The present invention relates to enzyme preparations consisting essentially of an enzyme which has cellulytic activity and comprises a first amino acid sequence having the following sequence and a second amino acid sequence having the following sequence wherein, at position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; at position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; at position 8 of the first sequence, the amino acid is Arg, Lys or His; at positions 9, 10, 12 and 14, respectively, of the first sequence, and at position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues with the provisos that, in the first amino acid sequence, (i) when the amino residue at position 12 is Ser, then the amino acid residue at position 14 is not Ser, and (ii) when the amino residue at position 12 is Gly, then the amino acid residue at position 14 is not Ala, performs very well in industrial applications such as laundry compositions, for biopolishing of newly manufactured textiles, for providing an abraded look of cellulosic fabric or garment, and for treatment of paper pulp. Further, the invention relates to DNA constructs encoding such enzymes, a method for providing a gene encoding for such enzymes, a method of producing the enzymes, enzyme preparations containing such enzymes, and the use of these enzymes for a number of industrial applications.

Endoglucanases

The present invention relates to xyloglucanases belonging to family 44 of glycosyl hydrolases and having a relative xyloglucanase activity of at least 30% between pH 5 and pH 8 are derived from the genus, especially from a strain oforsp. The xyloglucanases exhibit high performance in conventional detergent compositions.

Family 44 xyloglucanases

The present invention relates to a method for improving the properties of a cellulolytic enzyme by amino acid substitution, deletion or insertion, the method comprising the steps of:

Cellulase variants

The present invention relates to mannanases comprising e.g., a sequence of amino acids 32&#x2013;330 of SEQ ID NO: 2 or their homologues may be derived from e.g.,sp. I633, or may be encoded by polynucleotide molecules comprising a sequence of nucleotides 94&#x2013;990 of SEQ ID NO: 1 from, polynucleotide molecules that encode a polypeptide that is at least 65% identical to the sequence of amino acids 32&#x2013;330 of SEQ ID NO: 2, or degenerate nucleotide sequences thereof. The mannanases are alkaline and are useful e.g. in cleaning compositions, in a fracturing fluid useful to fracture a subterranean formation, for modifying plant material, and for treatment of cellulosic fibers.

Mannanases

The present invention relates to xyloglucanases belonging to family 44 of glycosyl hydrolases and having a relative xyloglucanase activity of at least 30% between pH 5 and pH 8 are derived from the genus , especially from a strain of or sp. The xyloglucanases exhibit high performance in conventional detergent compositions.

The present invention relates to variants of a cell-wall degrading enzyme having a beta-helix structure, which variant has at least one substituent in a position determined by identifying all residues potentially belonging to a stack; characterizing the stack as interior or exterior; characterizing the stack as polar, hydrophobic or aromatic/heteroaromatic based on the dominating characteristics of the parent or wild-type enzyme stack residues and/or its orientation relative to the beta-helix (interior or exterior); optimizing all stack positions of a stack either to hydrophobic aliphatic amino acids, hydrophobic aromatic or polar amino acids by allowing mutations within one or all positions to amino acids belonging to one of these groups; measuring thermostability of the variants by DSC or an application-related assay such as a Pad-Steam application test; and selecting the stabilized variants. Variant of a wild-type parent pectate lyase (EC 4.2.2.2) having the conserved amino acid residues D111, D141 or E141, D145, K165, R194 and R199 when aligned with the pectate lyase comprising the amino acid sequence of SEQ ID NO: 2 are preferred.

Cell-wall degrading enzyme variants

The present invention relates to xyloglucanases belonging to family 5 of glycosyl hydrolases are derived from strains of Paenibacillus, especially from strains of . The xyloglucanases show high performance in conventional liquid detergent compositions.

Family 5 xyloglucanases

The invention relates to a ellulose film comprising microfibrillated cellulose and to the use of it for screening of a biological compound and nucleic acids encoding a biological compound.

Cellulose films for screening

A variant of a cell-wall degrading enzyme having a beta-helix structure, which variant holds at least one substituent in a position determined by identifying all residues potentially belonging to a stack; characterising the stack as interior or exterior; characterising the stack as polar, hydrophobic or aromatic/heteroaromatic based on the dominating characteristics of the parent or wild-type enzyme stack residues and/or its orientation relative to the beta-helix (interior or exterior); optimizing all stack positions of a stack either to hydrophobic aliphatic amino acids, hydrophobic aromatic or polar amino acids by allowing mutations within one or all positions to amino acids belonging to one of these groups; measuring thermostability of the variants by DSC or an application-related assay such as a Pad-Steam application test; and selecting the stabilized variants. Variant of a wild-type parent pectate lyase (EC 4.2.2.2) having the conserved amino acid residues D111, D141 or E141, D145, K165, R194 and R199 when aligned with the pectate lyase comprising the amino acid sequence of SEQ ID NO: 2 are preferred.

An isolated or purified polypeptide having xyloglucanase activity which is obtained from a strain of the genus Malbranchea and has xyloglucanase activity in the pH range 4-11, measured at 50&deg; C.; and/or a molecular mass of 25&plusmn;10 kDa, as determined by SDS-PAGE; and/or an isoelectric point (pI) in the range 3-5; and/or an N-terminal sequence Ala-Asp-Phe-Cys-Gly-Gln-Xaa-Asp-Ser-Glu-Gln-Ser-Gly-Pro-Tyr-Ile-Val-Tyr-Asn-Asn-Leu is useful in industrial applications such as in laundry detergent compositions and for treatment of textiles.

Xyloglucanase from Malbranchea

Sanitary paper with improved softness (lower stiffness) can be obtained without significant loss of paper strength by using a papermaking pulp which is treated with a certain type of cellulase component. The cellulase component in question is characterized by not containing a cellulose-binding domain (CBD), and is more effective for making softer sanitary paper than a conventional cellulase preparation which contains a mixture of various cellulase components with and without a CBD.

Method of making sanitary paper from chemical pulp using a single component cellulase that does not contain cellulose-building domain

Growing community of inventors

Copenhagen, Denmark

Martin Schulein