Production of Lipase from Streptomyces spp. AM9-01 by Solid-State Fermentation of Residual Babassu Mesocarp and Immobilization in Accurel® MP1000

A wide range of agro-industrial waste has been generated due to higher demands for food and energy. New protocols for its valorization are urgent strategies for sustainable development. In this work, residual babassu mesocarp, a native plant from the north of Brazil, was used as a matrix for producing lipases through solid-state fermentation (SSF) by actinobacterial strains. Initially, 121 strains were screened by rhodamine B and tributyrin methods, where strain Streptomyces spp. AM9-01 was the most promising. It was submitted to the SSF at 30 °C, where 84.8 ± 1.5 U·mL−1 of hydrolytic activity (HA) was found in 48 h. Further studies at pH 7 increased lipase production, achieving 94.6 ± 1.6 U·mL−1 of HA in 12 h. The enzymatic extract was immobilized in Accurel® MP1000, where the biocatalyst Lip 10 showed 79.9 ± 1.5% immobilization efficiency, 4234 ± 24 U·g−1 of HA, and activity retention of 55.4%. Lip10 was used to synthesize ethyl oleate, showing conversions of over 97% in 6 h of reaction, while the commercial biocatalysts TLIM® and N435® showed conversions of over 95% in just 8 h. In addition, Lip10 showed operational stability for eight consecutive cycles. Therefore, it was demonstrated that babassu mesocarp is a viable alternative for obtaining competitive biocatalysts containing lipases for industrial applications from SSF by actinobacteria, which have few reports in the literature and could be potential biocatalytic agents.

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Journal
Reactions
Published
2025-02-04
DOI
https://doi.org/10.3390/reactions6010011
Citations
1
Primary Topic
Enzyme Catalysis and Immobilization
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article
Field-Weighted Citation Impact
0.81

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article

Production of Lipase from Streptomyces spp. AM9-01 by Solid-State Fermentation of Residual Babassu Mesocarp and Immobilization in Accurel® MP1000

Melissa Limoeiro Estrada Gutarra, Aldo Arrais, Ivaldo Itabaiana, Rodrigo Pires do Nascimento et al.
1 citations
Reactions
Enzyme Catalysis and Immobilization
0.81
article

Production of Lipase from Streptomyces spp. AM9-01 by Solid-State Fermentation of Residual Babassu Mesocarp and Immobilization in Accurel® MP1000

Melissa Limoeiro Estrada Gutarra, Aldo Arrais, Ivaldo Itabaiana, Rodrigo Pires do Nascimento, Tamires N. dos Anjos
article en
1 citations

Abstract

A wide range of agro-industrial waste has been generated due to higher demands for food and energy. New protocols for its valorization are urgent strategies for sustainable development. In this work, residual babassu mesocarp, a native plant from the north of Brazil, was used as a matrix for producing lipases through solid-state fermentation (SSF) by actinobacterial strains. Initially, 121 strains were screened by rhodamine B and tributyrin methods, where strain Streptomyces spp. AM9-01 was the most promising. It was submitted to the SSF at 30 °C, where 84.8 ± 1.5 U·mL−1 of hydrolytic activity (HA) was found in 48 h. Further studies at pH 7 increased lipase production, achieving 94.6 ± 1.6 U·mL−1 of HA in 12 h. The enzymatic extract was immobilized in Accurel® MP1000, where the biocatalyst Lip 10 showed 79.9 ± 1.5% immobilization efficiency, 4234 ± 24 U·g−1 of HA, and activity retention of 55.4%. Lip10 was used to synthesize ethyl oleate, showing conversions of over 97% in 6 h of reaction, while the commercial biocatalysts TLIM® and N435® showed conversions of over 95% in just 8 h. In addition, Lip10 showed operational stability for eight consecutive cycles. Therefore, it was demonstrated that babassu mesocarp is a viable alternative for obtaining competitive biocatalysts containing lipases for industrial applications from SSF by actinobacteria, which have few reports in the literature and could be potential biocatalytic agents.

ReactionsVol. 6(1)
Universidade Federal do Rio de Janeiro (BR)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico, Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro, Universidade Federal do Rio de Janeiro
Openalex Percentile: Top 31%
Enzyme Catalysis and Immobilization
0.81
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