Purification and some properties of endopolygalacturonase fromRhizopussp. LKN

✍ Scribed by F. B. Elegado; Y. Fujio

• Book ID: 104764942
• Publisher: Springer
• Year: 1994
• Tongue: English
• Weight: 245 KB
• Volume: 10
• Category: Article
• ISSN: 1573-0972
• DOI: 10.1007/bf00414857

✦ Synopsis

An endopolygalacturonase of Rhizopus sp. strain LKN, one of several isolates from tempe starter (rag/), was purified 235-fold by CM-Sephadex C-50, DEAE-Sephadex A-50 ion exchange chromatographies and Sephadex G-75 gel filtration. The purified enzyme was homogeneous by SDS-PAGE with a M r of 38.5 kDa. Its Km value for pectic acid was 2 mg/ml. It was stable at pH 4.5 to 11 and up to 50°C, with optimum activity at pH 4.5 to 4.75 and 55 to 60°C. Some ionic compounds enhanced the enzyme activity, whereas tannic acid at 0.5 raM caused about 90% inhibition.