A cold-active pectin lyase from the psychrophilic and basidiomycetous yeast Cystofilobasidium capitatum strain PPY-1.
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.
Nakagawa
Tomoyuki
T
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
Nagaoka
Toshinori
T
Miyaji
Tatsuro
T
Tomizuka
Noboru
N
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
D011133:Polysaccharide-Lyases; C027349:pectin lyase