Scholarlink

<p>Algeria imports all of its enzymes for use in different fields, which causes a ‎serious economic problem as the cost of these enzymes is continuously rising. New enzymes with efficient and unique properties are always sought to meet the specific needs of various industry sectors. This study aimed to investigate the purification and characterization of α-amylase from the Algerian <i>Geotrichum candidum</i> PO27, and its potential application as a desizing agent in the textile industry. This enzyme was purified 6.73-fold in two process steps: concentration by ultrafiltration, followed by exclusion ‎chromatography, achieving a final recovery of 9.1%. The results showed that its molecular weight was estimated for the first time by SDS-‎PAGE as 19.2&#xa0;kDa. Physicochemical characterization of purified enzyme revealed optimal activity at pH 5 and 70&#xa0;°C, thermostability properties, and high stability in the presence of Mg<sup>2+</sup> and Tween 80. It was also found to be resistant to surfactants and organic solvents. The enzyme exhibited a maximum velocity (V<sub>max</sub>) of 588.23 U/mL ‎and a high affinity for soluble starch, with a Michaelis Menten constant (K<sub>m</sub>) of 0.114&#xa0;mg/mL, values not previously reported. The enzyme showed notable efficacy in cotton desizing at room temperature, demonstrating its potential for efficient, low-cost industrial applications.</p> Graphical abstract <p></p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Purification and biochemical characterization of a novel thermostable acid α-amylase from Geotrichum candidum PO27 with industrial application

  • 期刊论文

  • 发表日期：

    2025年11月22日

查看全文
  • Ibtissem Chaib,
  • Scheherazed Dakhmouche-Djekrif,
  • Sonia Lorrai,
  • David Cannella,
  • Tahar Nouadri

摘要

Algeria imports all of its enzymes for use in different fields, which causes a ‎serious economic problem as the cost of these enzymes is continuously rising. New enzymes with efficient and unique properties are always sought to meet the specific needs of various industry sectors. This study aimed to investigate the purification and characterization of α-amylase from the Algerian Geotrichum candidum PO27, and its potential application as a desizing agent in the textile industry. This enzyme was purified 6.73-fold in two process steps: concentration by ultrafiltration, followed by exclusion ‎chromatography, achieving a final recovery of 9.1%. The results showed that its molecular weight was estimated for the first time by SDS-‎PAGE as 19.2 kDa. Physicochemical characterization of purified enzyme revealed optimal activity at pH 5 and 70 °C, thermostability properties, and high stability in the presence of Mg2+ and Tween 80. It was also found to be resistant to surfactants and organic solvents. The enzyme exhibited a maximum velocity (Vmax) of 588.23 U/mL ‎and a high affinity for soluble starch, with a Michaelis Menten constant (Km) of 0.114 mg/mL, values not previously reported. The enzyme showed notable efficacy in cotton desizing at room temperature, demonstrating its potential for efficient, low-cost industrial applications.

Graphical abstract