Purification and characterization of an extracellular β-glucosidase produced by phoma sp. KCTC11825BP isolated from rotten mandarin peel

Jung Youn Choi, Ah Reum Park, Yong Jin Kim, Jae Jin Kim, Chang Jun Cha, Jeong Jun Yoon

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

A β-glucosidase from Phoma sp. KCTC11825BP isolated from rotten mandarin peel was purified 8.5-fold with a specific activity of 84.5 U/mg protein. The purified enzyme had a molecular mass of 440 kDa with a subunit of 110 kDa. The partial amino acid sequence of the purified β-glucosidase evidenced high homology with the fungal β-glucosidases belonging to glycosyl hydrolase family 3. Its optimal activity was detected at pH 4.5 and 60oC, and the enzyme had a half-life of 53 h at 60oC. The Km values for p-nitrophenyl-β-D-glucopyranoside and cellobiose were 0.3 mM and 3.2 mM, respectively. The enzyme was competitively inhibited by both glucose (Ki=1.7 mM) and glucono-δ-lactone (Ki=0.1 mM) when pNPG was used as the substrate. Its activity was inhibited by 41% by 10 mM Cu2+ and stimulated by 20% by 10 mM Mg2+.

Original languageEnglish
Pages (from-to)503-508
Number of pages6
JournalJournal of microbiology and biotechnology
Volume21
Issue number5
DOIs
Publication statusPublished - 2011 May

Keywords

  • Characterization
  • Identification
  • Phoma sp.
  • Purification
  • β-glucosidase

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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