Journal
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
Volume 42, Issue -, Pages 193-196Publisher
WILEY
DOI: 10.1042/BA20040190
Keywords
cold-active enzyme; Cystofilobasidium copitatum; esterification; pectin lyase; psychrophile; substrate specificity
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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-I. The purified PNL has a molecular mass of approx. 42 kDa, and its N-terminal amino acid sequence is ATGVTGSAYGFATGTTGGG-SATPAY, which exhibits 72% identity with that of PNLF from Aspergillus niger. The purified PNL exhibited high activity at WC. although its optimum temperature was 40 degrees C. Moreover, K-m and V-max 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-I is a cold-active PNL that is able to degrade pectin compounds at low temperature.
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