Polypeptide

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

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Details

C435S069100, C435S200000, C435S201000, C435S183000, C536S023740

Reexamination Certificate

active

10864874

ABSTRACT:
We disclose a PS4 variant polypeptide derivable from a parent polypeptide, the parent polypeptide having non-maltogenic exoamylase activity, which PS4 variant polypeptide comprises one or more of the following substitutions: G69P, A141P, G223A, A268P, G313P, S399P and G400P, with reference to the position numbering of aPseudomonas saccharophiliaexoamylase sequence shown as SEQ ID NO: 1. Such PS4 variant polypeptides may be used as exo-amylases, particularly as non-maltogenic exoamylases. Combinations of such PS4 variant polypeptides together with Novamyl are disclosed.

REFERENCES:
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patent: WO 99/50399 (1999-10-01), None
patent: WO 02/068589 (2002-09-01), None
Christophersen et al., “Enzymatic Characterisation of Novamyl®, a Thermostable α-Amylase,” Starch Starke, Wiley-VCH Verlag, DE, vol. 50, No. 1, 1998, pp. 39-45.
Zhou, J. et al, “Nucleotide sequence of the maltotetraohydrolase gene fromPseudomonas saccharophila,” FEBS Letters, vol. 255, 1989, pp. 37-41.
Fogarty, W., 1983, Microbial Amylases, W.M. Fogarty (Ed.) Microbial enzymes and biotechnology, Applied Sicence, London, pp. 1-92.
Fogarty, W. et al, “Starch-Degrading Enzymes of Microbial Origin,” M.J. Bull (Ed.), Progress in Industrial Microbiology, vol. 15, Elsevier Scientific, 1979, pp. 87-150.
Kainuma, K. et al, “Isolation and action pattern of maltohexaose producing amylase fromaerobacter aerogenes,” FEBS Letters, vol. 26, No. 1, Oct. 1972, pp. 281-285.

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