TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preparation: (I) is prepared by (a) culturing a strain in its wild-state capable of producing (I), (b) culturing (VI) under conducive conditions for the production of (I) or (c) culturing (VII) under conditions conducive for production of (I), and recovering (I) (claimed).Preferred Polypeptide: (I) is an enzyme having at least minor activity against a substrate chosen from oat xylan, birchwood xylan and wheat arabinoxylan. (I) in its natural form comprises conserved regions of His at position 1, Ala or Pro at position 59 or 76, Gly at position 60 or 75, Trp or Phe at position 100, Thr or Phe at position 101, Lys or Cys at position 102, Ile, Val or Leu at position 103 or 148, Leu, Ile, Val or Met at position 130, 140 or 141, Pro at position 131, Gly, Xaa and Tyr at position 137-139, Arg at position 142, Glu or Gln at position 143-144, His or Asn at position 149, Cys at position 163, and Pro and Gly at position 209-211. (I) comprises a fully defined sequence of 233 (S1), 319 (S2) and 220 (S3) amino acids as given in the specification, its allelic variant or its fragment, which has an anti-staling effect in an edible product. (I) has at least 65% identity to (S1)-(S3) or 10 amino acids of (S1)-(S3). (I) comprises at least one substitution , deletion or insertion outside the conserved portions of amino acid sequence, or one substitution inside the conserved portions. The number of substitution, deletion or insertion is 10. (I) is encoded by nucleotide sequences which hybridize under very low stringent conditions with a polynucleotide probe chosen from complementary strand of nucleotides or cDNA sequence contained in nucleotides of 52-699 of a fully defined sequence of 699 (S4) nucleotides as given in the specification, 46-957 of a fully defined sequence of 957 (S5) nucleotides as given in the specification or 58-660 of a fully defined sequence (S6) of 660 nucleotides as given in the specification, complementary strand of nucleotides 46-857 of (S5), or complementary strand of nucleotides 52-300 or 301-699 of (S4), 46-501 or 502-957 of (S5), or 58-300 or 301-660 of (S6). (I) encoded by nucleotide sequence comprises nucleotides 52-699 of (S4), 46-957 of (S5) or 58-660 of (S6) or sequences differing from 52-699 of (S4), 46-957 of (S5) or 58-660 of (S6) by virtue of the degeneracy of the genetic code. (I) is obtained from fungus.Preferred Composition: (II) is in the form of granules having a particle size distribution with more than 95% (by weight) of the particles in the range of 25-500 microm. (II) comprises 0.5-100 mg/kg of (I) and maltogenic exo-amylase. (II) is a dough composition.Preferred Polynucleotide: (IV) comprise a subsequence (S4)-(S6) that encodes a fragment of (S1)-(S3) having an anti-staling effect in edible products and comprises conserved regions. (IV) comprises nucleotide sequence encoding (S1)-(S3) or its mature polypeptide. (IV) comprises at least one mutation in the regions of (S4)-(S6) that encodes mature polypeptide having His at position 1, Ala or Pro at position 59 or 76, Gly at position 60 or 75, Trp or Phe at position 100, Thr or Phe at position 101, Lys or Cys at position 102, Ile, Val or Leu at position 103 or 148, Leu, Ile, Val or Met at position 130, 140 or 141, Pro at position 131, Gly, Xaa and Tyr at position 137-139, Arg at position 142, Glu or Gln at position 143-144, His or Asn at position 149, Cys at position 163, and Pro and Gly at position 209-211. (IV) comprises a nucleotide sequence which has at least 65% identity with 52-699 of (S4), 46-957 of (S5) or 58-660 of (S6). EXAMPLE - To prepare glycoside hydrolase-61 (GH-61), the following test was done. A culture supernatant from a fermentation of Aspergillus oryzae strain expressing a fully defined sequence of 699 nucleotides as given in the specification, was filtered through a 0.22 microns filter to remove the mycelia. About 350 ml of the filtered supernatant was diluted to 1450 ml with water and pH adjusted to 7.5 resulting in a conductivity of 1.8 mS/cm. This solution was loaded onto a 50 ml Q-Sepharose anion exchange column exchange column equilibrated with 25 nM Tris (pH 7.5). The column was washed with 15 column volumes of 25 nM over 20 column volumes. From sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) it was seen that a polypeptide with a molecular weight of 29 kDa was eluted during the wash with 25 nM Tris. Fractions containing the 29 kDa were pooled and concentrated on an Amicon ultrafiltration device with a 6 kDa cut off filter. The concentrated pool was at least 95% pure as estimated from SDS-PAGE and N-terminal sequencing of the polypeptide gave the sequence corresponding to a fully defined sequence of 233 amino acids as given in the specification (His-Tyr-Thr-Phe-Pro-Gln-Thr-Asp-Ile-Asn-Gly-Gln-Leu-Ser-Gly-Glu).