Purification and Characterization of a β-N-Acetylhexosaminidase from Wheat Bran and Its Applicability to Biocontrol of Fusarium solani
2012
Ju, W.T., Chonnam National University, Gwangju, Republic of Korea | Nguyen, Van Nam, Tay Nguyen University, Buon Ma Thuot, Vietnam | Jung, W.J., Chonnam National University, Gwangju, Republic of Korea | Kim, K.Y., Chonnam National University, Gwangju, Republic of Korea | Park, R.D., Chonnam National University, Gwangju, Republic of Korea
N-acetyl-β-D-hexosaminidase was purified from wheat bran and characterized. The purified enzyme showed two protein bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) with molecular mass of 75 and 78 kDa. The enzyme exhibited optimum pH and temperature at 5.0 and 50℃, respectively. The enzyme was active on the substrates of p-nitrophenyl-N-acetyl-β-D-glucosaminide (pNP-GlcNAc) and p-nitrophenyl-N-acetyl-β-D-galactosaminide (pNP-GalNAc), whereas inactive on pNP-β-D-glucopyranoside, pNP-β-D-galactopyranoside, swollen chitin, and colloidal chitin, suggesting high substrate specificity. The enzyme activity for pNP-GlcNAc was stable at pH 3-6 and under 50℃. The K∧m, V∧max and K∧cat for pNP-GlcNAc were 0.014 mM, 0.05 μmol/min, and 3.01×10∨6 min-¹, respectively. The enzyme could be completely inhibited at 1-10 mM HgCl₂ and AgNO₃, suggesting that the intact thiol group is essential for activity. β-N-Acetylhexosaminidase from wheat bran could inhibit the conidial germination and digest the hyphae of Fusarium solani.
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