Kinetic characterization of laccase from Bacillus atrophaeus, and its potential in juice clarification in free and immobilized forms

Narnoliya, Lokesh Kumar; Agarwal, Neera; Patel, Satya Narayan; Singh, Sudhir P.

doi:10.1007/s12275-019-9170-z

Cited by 22 publications

(15 citation statements)

References 40 publications

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“…In recent years, numerous bacterial strains with metabolic capabilities to utilize lignin and its derivatives have been isolated from the genus Bacillus , e.g. Bacillus pumilus 21 , 22 , Bacillus atrophaeus 23 , 24 . Most of these organisms have been tested to possess pathways for the catabolism of lignin and its aromatic derivatives such as catechol, alkyl catechols, vanillin, and guaiacol as their sole carbon source for growth.…”

Section: Introductionmentioning

confidence: 99%

A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement

Adewale

Lang

Huang

et al. 2021

Sci Rep

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Identification of novel enzymes from lignin degrading microorganisms will help to develop biotechnologies for biomass valorization and aromatic hydrocarbons degradation. Bacillus ligniniphilus L1 grows with alkaline lignin as the single carbon source and is a great candidate for ligninolytic enzyme identification. The first dioxygenase from strain L1 was heterologously expressed, purified, and characterized with an optimal temperature and pH of 32.5 °C and 7.4, respectively. It showed the highest activity with 3-ethylcatechol and significant activities with other substrates in the decreasing order of 3-ethylcatechol > 3-methylcatechol > 3-isopropyl catechol > 2, 3-dihydroxybiphenyl > 4-methylcatechol > catechol. It did not show activities against other tested substrates with similar structures. Most reported catechol 2,3-dioxygenases (C23Os) are Fe2+-dependent whereas Bacillus ligniniphilus catechol 2,3-dioxygenase (BLC23O) is more Mn2+- dependent. At 1 mM, Mn2+ led to 230-fold activity increase and Fe2+ led to 22-fold increase. Sequence comparison and phylogenetic analyses suggested that BL23O is different from other Mn-dependent enzymes and uniquely grouped with an uncharacterized vicinal oxygen chelate (VOC) family protein from Paenibacillus apiaries. Gel filtration analysis showed that BLC23O is a monomer under native condition. This is the first report of a C23O from Bacillus ligniniphilus L1 with unique substrate preference, metal-dependency, and monomeric structure.

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Section: Introductionmentioning

confidence: 99%

A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement

Adewale

Lang

Huang

et al. 2021

Sci Rep

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“…The treatment with immobilized laccase improved the sensory profile of the juice thanks to the reduction of the vinyl guaiacol concentration, a compound described as having a spicy/peppery aroma and which is considered a potent off-flavor. A similar improvement in the sensory profile of plant juices was obtained when an immobilized recombinant laccase from Bacillus atrophaeus Nakamura, expressed in Escherichia coli onto magnetic nanoparticles, was used for the removal of phenolics with consequent clarification of banana pseudo-stem juice, sorghum stem juice, and apple fruit juice (Narnoliya, Agarwal, Patel, & Singh, 2019). A laccase from the fungus Abortiporus biennis (Bull.)…”

Section: Laccases In the Beverage Industrymentioning

confidence: 70%

Laccases in food processing: Current status, bottlenecks and perspectives

Backes

Kato

Corrêa

et al. 2021

Trends in Food Science & Technology

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“…To investigate the factors affecting the flavonoid yield, fermentations were performed with different initial pH levels (5, 6, 7, 8, and 9), temperatures (25, 30, 35, 37, 40 °C), leaf powder concentrations (1-5 g L −1 ), and fermentation times (12,24,36,48,60,72, and 84 h). All the experiments, under different conditions, were performed in triplicated.…”

Section: Single Factors Optimizationmentioning

confidence: 99%

“…Several studies have shown their potential in extracting various types of value‐added and bioactive compounds such as phenolic compounds, 34 carbohydrates, 35 fruit juice, 36 and pigments 37 . So far, many fungi and bacteria have been found capable of producing lignocellulolytic enzymes such as cellulases, 38–41 hemicellulases, 42–44 peroxidases, and laccases 45–49 …”

Section: Introductionmentioning

confidence: 99%

“…37 So far, many fungi and bacteria have been found capable of producing lignocellulolytic enzymes such as cellulases, [38][39][40][41] hemicellulases, [42][43][44] peroxidases, and laccases. [45][46][47][48][49] The utilization of lignocellulolytic enzymes could contribute to improving the extraction of flavonoids from Ginkgo biloba, 26,27,50,51 and fermentation using lignocellulosedegrading microorganisms could be another innovative approach to improving the extraction of Ginkgo biloba flavonoids. The flavonoids are usually linked with pectin and hemicellulose.…”

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confidence: 99%

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Extracting flavonoid from Ginkgo biloba using lignocellulolytic bacteria Paenarthrobacter sp. and optimized via response surface methodology

Han

Chio²,

et al. 2021

Biofuels Bioprod Bioref

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Ginkgo biloba flavonoids are important natural bioactive compounds with strong physiological effects. To develop an eco‐friendly and effective method for extracting flavonoids from plants, a microbial method involving lignocellulose‐degrading bacterial enzymes was developed to improve flavonoid extraction from Ginkgo biloba leaves. In this study, a newly isolated bacterial strain, Paenarthrobacter sp. S1.3, was employed for the fermentation processing of Ginkgo biloba leaf powder. The enzymatic characteristics of xylanase, CMCase, polygalacturonase, and β‐glucosidase from Paenarthrobacter sp. S1.3 were also investigated. The major fermentation parameters for the microbial extraction of Ginkgo biloba flavonoids were optimized using response surface methodology. Under optimal conditions (30.6 °C, initial pH 7.6, and fermentation time 25 h), a total flavonoid yield of 34.15 ± 0.52 mg g−1 dry weight was obtained, which was 2.11 fold and 1.42 fold higher than the yields obtained from the unfermented and ethanol extraction methods, respectively. The optimized results also suggest that the polygalacturonase and β‐glucosidase might play an important role in flavonoid extraction. Fermentation utilizing lignocellulose‐degrading bacteria was a feasible green approach to improve the extraction of natural compounds from plants. © 2021 Society of Chemical Industry and John Wiley & Sons, Ltd

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Kinetic characterization of laccase from Bacillus atrophaeus, and its potential in juice clarification in free and immobilized forms

Cited by 22 publications

References 40 publications

A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement

A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement

Laccases in food processing: Current status, bottlenecks and perspectives

Extracting flavonoid from Ginkgo biloba using lignocellulolytic bacteria Paenarthrobacter sp. and optimized via response surface methodology

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