| Literature DB >> 15847609 |
Tomoyuki Nakagawa1, Toshinori Nagaoka, Tatsuro Miyaji, Noboru Tomizuka.
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.Entities:
Mesh:
Substances:
Year: 2005 PMID: 15847609 DOI: 10.1042/BA20040190
Source DB: PubMed Journal: Biotechnol Appl Biochem ISSN: 0885-4513 Impact factor: 2.431