Novozymes A/s

Sanne O Schroder Glad

Allan Svendsen

Jesper Vind

Kim Borch

Shamkant Anant Patkar

Claus Crone Fuglsang

Gitte Budolfsen

Kirsten Bojsen

Andreas Petri

Kirk Matthew Schnorr

Lene Nonboe Andersen

Markus Sakari Kauppinen

Lars Kongsbak

Niels Erik Krebs Lange

Signe Munk

Carsten Schau Andersen

Tomoko Matsui

Martin Schulein

Steffen Danielsen

Shiro Fukuyama

Mads Eskelund Bjornvad

Martin Sch&uuml;lein

Mads Eskelund Bj&oslash;rnvad

Stefan Minning

Hanne Dela, Legal Representative

Soren Moller

S&oslash;ren M&oslash;ller

Torben Peter

The substrate specificity of a lipolytic enzyme can be modified by making alterations to the amino acid sequence in a defined region of the lipolytic enzyme, so as to increase the level of a desired activity or to decrease the level of an undesired activity. Thus, the inventors have developed lipolytic enzyme variants with a modified amino acid sequence with a substrate specificity which can be tailored for specific uses.

Lipolytic enzyme variants

Attaching a peptide extension to the C-terminal amino acid of a lipase reduces the tendency to form odor. This may lead to lipase variants with a reduced odor generation when washing textile soiled with fat which includes relatively short-chain fatty acyl groups (e.g., up to C) such as dairy stains containing butter fat or tropical oils such as coconut oil or palm kernel oil.

Lipase variants

The present invention relates to lipolytic enzyme variants with improved thermostability are obtained by substituting certain specified amino acid residues in a fungal lipolytic enzyme. The thermostable lipolytic enzyme variants are useful, e.g., for controlling pitch troubles in a process for the production of mechanical pulp or a paper-making process using mechanical pulp.

Lipolytic enzyme variant

Attaching a peptide extension to the C-terminal amino acid of a lipase re-duces the tendency to form odor. This may lead to lipase variants with a reduced odor generation when washing textile soiled with fat which includes relatively short-chain fatty acyl groups (e.g. up to C8) such as dairy stains containing butter fat or tropical oils such as coconut oil or palm kernel oil.

The present invention relates to pectate lyases comprising the amino acid sequence Asn Leu Asn Ser Arg Val Pro (NLNSRVP) (amino acids 236&#x2013;242 of SEQ ID NO: 2) belonging to Familyof 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 fromspecies.

Pectate lyases

Variants of fungal cutinases having improved thermostability comprise substitution of one or more specified amino acid residues and/or a specified N-terminal extension. The variants may optionally comprise additional alterations at other positions.

Cutinase variants

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 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.

Growing community of inventors

Ballerup, Denmark

Sanne O Schroder Glad