1887

Abstract

Summary: An intracellular pectinolytic enzyme was isolated from a cell extract of and purified. The optimum pH for enzyme activity was 5·6. The enzyme preferentially degraded de-esterified substrates by hydrolysis of monosaccharide units from the non-reducing end; the only product of degradation was D-galacturonic acid. Values of and for oligo- and polygalacturonates indicated that the best substrate was digalacturonic acid; oligogalact-uronates containing either a saturated or a Δ4,5-unsaturated non-reducing end were both degraded. The enzyme was classified as an exo-D-galacturonanase [poly(1,4-α-D-galacturonide) galacturonohydrolase (EC 3.2.1.67)].

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/content/journal/micro/10.1099/00221287-131-8-2053
1985-08-01
2019-10-17
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-131-8-2053
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