Novozymes A/s

Novo Nordisk A/s

Other

Mads Eskelund Bj&oslash;rnvad

Martin Sch&uuml;lein

Kirk Matthew Schnorr

Lars Kongsbak

Niels Erik Krebs Lange

Lene Nonboe Andersen

Markus Sakari Kauppinen

S&oslash;ren M&oslash;ller

Sanne O Schr&oslash;der Glad

Philip Anwar Husain

Martin Sh&uuml;lein

Martin Schulein

Ib Groth Clausen

Jack Bech Nielsen

Sanne O Schroder Glad

Lisbeth Bech

Reinhard Wilting

Peter Rahbek &Oslash;stergaard

Jens Toenne Andersen

Carsten Sj&oslash;holm

Mariko Hatakeyama

The present invention relates to pectate lyases comprising the amino acid sequence Asn Leu Asn Ser Arg Val Pro (NLNSRVP) (SEQ ID NO: 2) belonging to Family 1 of polysaccharide lyases have good performance in industrial processes under neutral or alkaline conditions such as laundering and textile processing. The pectate lyase may be derivable from Bacillus species.

Pectate lyases

The present invention provides methods for high-temperature biopreparation of cellulosic fibers by contacting the fibers with pectin-degrading enzymes, preferably thermostable, alkaline, divalent cation-independent pectate lyases, under conditions compatible with scouring and bleaching technologies.

Biopreparation of textiles at high temperatures

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

Novel mannanases comprising e.g. an amino acid sequence as shown in positions 31-330 of SEQ ID NO:2 or their homologues may be derived from e.g. Bacillus sp. I633, or may be encoded by polynucleotide molecules comprising a nucleotide sequence as shown in SEQ ID NO: 1 from nucleotide 91 to nucleotide 990, polynucleotide molecules that encode a polypeptide that is at least 65% identical to the amino acid sequence of SEQ ID NO: 2 from amino acid residue 31 to amino acid residue 330, 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

Pectin degrading enzymes derived from or endogeneous to or other Bacillus species which are at least 99% homologous to based on aligned 16S rDNA sequences have optimum activity at pH higher than 8. The pectin degrading enzymes belongs to the enzyme classes pectate lyases (EC 4.2.2.2), pectin lyases (EC 4.2.2.10) and polygalacturonases (EC 3.2.1.15) and are useful in industrial processes under alkaline conditions such as in textile processing and as an active ingredient eg in laundry detergents and hard surface cleaning products.

Pectin degrading enzymes from Bacillus licheniformis

A novel pectate lyase belonging to a novel family of polysaccharide lyases has good performance in industrial processes under neutral or alkaline conditions such as laundering and textile processing. The pectate lyase may be derivable from Bacillus species.

A novel group of pectate lyases comprising the amino acid sequence Asn Leu Asn Ser Arg Val Pro (NLNSRVP) belonging to Family 1 of polysaccharide lyases have good performance in industrial processes under neutral or alkaline conditions such as laundering and textile processing. The pectate lyase may be derivable from Bacillus species.

The invention relates to a method for modifying animal feed, in particular animal feed containing plant material such as soybean, by adding to the animal feed at least one galactanase enzym, to a method for obtaining a DNA sequence encoding a galactanase enzyme or a portion thereof, and to isolated polynucleotide molecules encoding polypeptides having galactanase activity.

Bacterial galactanases and use thereof

The present invention provides methods for higha-temperature biopreparation of cellulosic fibers by contacting the fibers with pectin-degrading enzymes, preferably thermostable, alkaline, divalent cation-independent pectate lyases, under conditions compatible with scouring and bleaching technologies.

An enzyme preparation comprising an enzyme having endo-&bgr;-1,4-glucanase activity obtainable from or endogeneous to a strain belonging to the genus Saccharothrix such as,IFO 14444; an isolated polynucleotide (DNA) molecule encoding an enzyme or enzyme core (the catalytically active domain of the enzyme) exhibiting endo-&bgr;-1,4-glucanase activity selected from (a) polynucleotide molecules comprising a nucleotide sequence as shown in SEQ ID NO:1 from nucleotide 676 to nucleotide 1470, (b) polynucleotide molecules that encode a polypeptide that is at least 80% identical to the amino acid sequence of SEQ ID NO:2 from amino acid residue 226 to amino acid residue 490, and (c) degenerate nucleotide sequences of (a) or (b), the expressed endoglucanase and the enzyme preparation being useful in a detergent or fabric softener composition or in the textile industry for improving the properties of cellulosic fibres or fabric or for providing a stone-washed look of denim.

Endo-B-1,4-glucanases from saccharothrix

A novel group of pectate lyases comprising the amino acid sequence Asn Leu Asn Ser Arg Val Pro (NLNSRVP) belonging to Family 1 of polysaccharide lyases have good performance in industrial processes under neutral or alkaline conditions such as laundering and textile processing. The pectate lyase are derivable from Bacillus species.

Growing community of inventors

Frederiksberg, Denmark

Mads Eskelund Bjørnvad

Growing community of inventors

Frederiksberg, Denmark

Mads Eskelund Bj&oslash;rnvad

Mads Eskelund Bjørnvad