These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and Characterization of Thermostable α-Amylase from Soil Bacterium Bacillus sp.
    Author: Enez B.
    Journal: Protein Pept Lett; 2021; 28(12):1372-1378. PubMed ID: 34711150.
    Abstract:
    BACKGROUND: Amylases are used in several industrial and biotechnological sectors, including those producing textiles, detergents, paper and bakery products. OBJECTIVE: This study aimed to purify an industrially important α-amylase from Bacillus sp. For this purpose, a single and rapid α-amylase purification was performed using the starch affinity method. METHODS: Characterization of the purified enzyme was determined by investigating temperature, pH stability, detergents, and metal ions. RESULTS: The purification coefficient of 29.8-fold with a yield of 9.2% was found. The molecular weight of the purified α-amylase was determined to be 53 kDa by SDS-PAGE, and thermostability was confirmed with 100% activity at 30ºC and 40ºC after 1 h. The purified enzyme was stable over a wide range of pH values, with optimum activity at pH 6.0, 7.0 and 8.0 after 2 h. The study also investigated the effects of the metal ions and detergents on the purified amylase and found that Mg2+ and Ca2+ ions were the activators of the enzyme, while Zn2+, Co2+ and Na+ ions decreased the activity. Furthermore, Hg2+; indicated complete inhibition of amylase activity. The detergents Triton X-100 and Tween 20 increased the α-amylase activity, while sodium dodecyl sulfate inhibited the activity. CONCLUSION: The purified α-amylase obtained from Bacillus sp. is considered to be environmentally friendly, can be processed in a short time, and has a low cost.
    [Abstract] [Full Text] [Related] [New Search]