title: A cold-active pectin lyase from the psychrophilic and basidiomycetous yeast Cystofilobasidium capitatum strain PPY-1.
abstract: In the present study we purified a cold-active PNL (pectin lyase) from the extracellular fraction of the PPY (pectinolytic and psychrophilic yeast) Cystofilobasidium capitatum strain PPY-1. The purified PNL has a molecular mass of approx. 42 kDa, and its N-terminal amino acid sequence is ATGVTGSAYGFATGTTGGGSATPAY, which exhibits 72% identity with that of PNL F from Aspergillus niger. The purified PNL exhibited high activity at 10 degrees C, although its optimum temperature was 40 degrees C. Moreover, Km and Vmax for pectin as a substrate were found to have values 36.6 mg/ml and 3000 units/mg respectively. These findings may indicate that this enzyme from strain PPY-1 is a cold-active PNL that is able to degrade pectin compounds at low temperature.
authors.affiliation: Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri, Hokkaido 099-2493, Japan. t-nakaga@bioindustry.nodai.ac.jp
authors.forename: Tomoyuki
authors.initials: T
authors.lastname: Nakagawa
authors.forename: Toshinori
authors.initials: T
authors.lastname: Nagaoka
authors.forename: Tatsuro
authors.initials: T
authors.lastname: Miyaji
authors.forename: Noboru
authors.initials: N
authors.lastname: Tomizuka
mesh_terms: D000595:Amino Acid Sequence; D001234:Aspergillus niger / Q000201:enzymology; D001487:Basidiomycota / Q000201:enzymology* / Q000235:genetics; D003080:Cold Temperature; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011133:Polysaccharide-Lyases / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013696:Temperature; D014783:Viscosity / Q000187:drug effects
chemical_list: D011133:Polysaccharide-Lyases; C027349:pectin lyase