4.5 Article

Sustainable Production of Thermostable Laccase from Agro-Residues Waste by Bacillus aquimaris AKRC02

Journal

CATALYSIS LETTERS
Volume 152, Issue 6, Pages 1784-1800

Publisher

SPRINGER
DOI: 10.1007/s10562-021-03753-y

Keywords

Laccase; Bacillus aquimaris AKRC02; Agro-residues waste; Process parameters; Optimization; Stability

Funding

  1. University Grant Commission, New Delhi
  2. NFPwD [01-01/2019-Sch.]
  3. Department of Biotechnology New Delhi [BT/PR18896/BCE/8/1372/2016]

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A thermo-tolerant halophilic Bacillus aquimaris AKRC02 was isolated from pulp and paper mill waste sludge for efficient laccase production. Rice bran was found to support the maximum laccase production. Optimized environmental conditions and nutritional sources significantly enhanced laccase production, resulting in purified enzyme with high specific activity and thermal stability.
Laccase is a versatile enzyme that plays a major role in the remediation of various environmental pollutants. In this work, a thermo-tolerant halophilic Bacillus aquimaris AKRC02 was isolated from pulp and paper mill waste sludge for efficient laccase production. Various agro-industrial waste residues, including potato peel, banana peel, sawdust, pea peel, wheat bran, orange peel, and rice bran, were screened to produce laccase using a submerged fermentation process. Among these, rice bran supported the maximum laccase production (4.58 U/mL). The optimized environmental conditions (incubation time 120 h; 4.58 U/mL), 35 C-0; 6.624 U/mL) and pH 7.0; 10.142 U/mL) and nutritional sources (glucose 1.0%; 14.164 U/mL and peptone 0.5%; 18.124 U/mL) significantly enhanced the laccase production. Purified laccase showed a specific activity and purification fold of 228.34 U/mg and 38.08, respectively. The purified enzyme showed a molecular weight of 65 kDa and high thermal stability at 45 C-0 for 8 h. In conclusion, the remarkable properties of the newly isolated bacterium may provide a significant opportunity for degrading environmental contaminants, making it an attractive biocatalyst for industrial applications.

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