Production of Lignocellulolytic Enzymes by Microorganisms Isolated from Bulbitermes sp. Termite Gut in Solid-State Fermentation

Kamsani, Noratiqah; Salleh, Madihah Md.; Yahya, Adibah; Chong, Chun Shiong

doi:10.1007/s12649-015-9453-5

Cited by 31 publications

(20 citation statements)

References 63 publications

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“…The results revealed that peroxidase production by the test organism differ significantly (p < 0.05) when cultivated on the different substrates, with sawdust supporting the highest production (37.50 ± 0.00 U mg −1 ) while the lowest production was recorded with corn stover (3.76 ± 0.00 U mg −1 ). This result is in agreement with previous similar investigations [25,57,63], where high peroxidase activity was induced by sawdust as solid substrate under SSF. This finding could be linked to the inductive effect of the phenolic and non-phenolic constituents of sawdust.…”

Section: Assessment Of Agricultural Residues For Exoperoxidase Producsupporting

confidence: 94%

Exoproduction and Molecular Characterization of Peroxidase from Ensifer adhaerens

et al. 2019

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The increased industrial application potentials of peroxidase have led to high market demand, which has outweighed the commercially available peroxidases. Hence, the need for alternative and efficient peroxidase-producers is imperative. This study reported the process parameters for enhanced exoperoxidase production by Ensifer adhaerens NWODO-2 (accession number: KX640918) for the first time, and characterized the enzyme using molecular methods. Peroxidase production by the bacteria was optimal at 48 h, with specific productivity of 12.76 U mg−1 at pH 7, 30 °C and 100 rpm in an alkali lignin fermentation medium supplemented with guaiacol as the most effective inducer and ammonium sulphate as the best inorganic nitrogen source. Upon assessment of some agricultural residues as sources of carbon for the enzyme production, sawdust gave the highest peroxidase productivity (37.50 U mg−1) under solid-state fermentation. A search of the polymerase chain reaction (PCR)-amplified peroxidase gene in UniProtKB using blastx showed 70.5% similarity to an uncharacterized protein in Ensifer adhaerens but phylogenetic analysis suggests that the gene may encode a catalase-peroxidase with an estimated molecular weight of approximately 31 kDa and isoelectric point of about 11. The nucleotide sequence of the detected gene was deposited in the GenBank under the accession number MF374336. In conclusion, the ability of the strain to utilize lignocellulosic materials for peroxidase production augurs well for biotechnological application as this would greatly reduce cost, which is a major challenge in industrial enzyme production.

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Section: Assessment Of Agricultural Residues For Exoperoxidase Producsupporting

confidence: 94%

Exoproduction and Molecular Characterization of Peroxidase from Ensifer adhaerens

et al. 2019

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“…This is further corroborated by Kamsani et al. , who also reported high yields of manganese peroxidase and laccase by Bacillus species grown on sawdust under SSF. Nonetheless, the peroxidase activity on sawdust in this study is higher than what was achieved in the aforementioned studies as Knezevic et al.…”

Section: Resultssupporting

confidence: 78%

“… reported a manganese peroxidase activity of 1767.7 U L −1 for Trametes suaveolens whereas Kamsani et al. recorded 729.12 and 47.73 U g −1 as lignin peroxidase and manganese peroxidase–specific activities for Aspergillus sp. A1 and Bacillus sp.…”

Section: Resultsmentioning

confidence: 99%

Agrowastes utilization by Raoultella ornithinolytica for optimal extracellular peroxidase activity

Falade

Mabinya

Okoh

et al. 2018

Biotech and App Biochem

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The industrial applications and prospects of microbial peroxidase are on the upwards trend, thus necessitating the search for sources with high turnaround time. Actinobacterial species have been a major source of peroxidase for the obvious reasons of having robust metabolite expression capabilities. However, other bacteria species have been underexplored for peroxidase production, hence the motivation for the investigation into the peroxidase production potential of Raoultella ornithinolytica OKOH-1 (KX640917). The bacteria expressed optimum specific peroxidase activity of 16.48 ± 0.89 U mg −1 , which is higher than those previously reported. The optimal fermentation conditions were pH 5 (3.44 ± 0.64 U mL −1 ), incubation temperature of 35 • C (5.25 ± 0.00 U mL −1 ), and agitation speed of 150 rpm (9.45 ± 2.57 U mL −1 ), with guaiacol and ammonium chloride as the best inducer and nitrogen supplement, respectively. On valorization of agrowastes as a sole carbon source for the secretion of peroxidase, sawdust gave the best peroxidase yield (15.21 ± 2.48 U mg −1 ) under solid-state fermentation. Also, a nonperoxide-dependent enzyme activity, which suggests probable laccase activity, was observed. The ability of the bacteria to utilize agrowastes is highly economical and as well a suitable waste management strategy. Consequently, R. ornithinolytica OKOH-1 is a promising industrial strain with dexterity for enhanced peroxidase production.

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“…Pure xylan has been added in the agar medium for qualitative detection of xylanolytic micro-organisms by many researchers. Some workers have also used purified xylan to qualitatively screen xylanase enzyme from termite gut (Bastien et al 2013;Kamsani et al 2016). Upon further quantitative analysis of cellulose and xylan degrading enzymes, all 30 bacterial isolates isolated from termite gut displayed cellulase (CMCase) and xylanase activity in the range of 0.5-6.8 and 51-360 IU/ml, respectively, and all 30 bacterial isolates isolated from termitarium displayed cellulase (CMCase) and xylanase activity in the range of 0.45-6.02 and 55-380 IU/ml, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…There are only few reports of their combined production, till date. The use of purified substrates like xylan (Bastien et al 2013;Kamsani et al 2016) and cellulose (Bashir et al 2013) has been done by many workers for qualitative estimation of enzyme activity during screening of xylanase and cellulase producing microbes from termite gut microbiome and has been found to be very expensive. Kaur et al (2011) have replaced the use of highly expensive substrates by agricultural wastes for screening purposes.…”

Section: Introductionmentioning

confidence: 99%

Cost-effective screening and isolation of xylano-cellulolytic positive microbes from termite gut and termitarium

et al. 2017

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In this study, screening and isolation of xylanocellulolytic enzymes producing positive microbes from termitarium and termite gut microbiome were done using cost-effective agricultural wastes. The enrichment of xylano-cellulolytic microbes was done in three steps using wheat bran and waste paper. The qualitative screening of xylanase and cellulase producing micro-organisms was done on nutrient agar plates containing wheat bran and waste paper, respectively. Xylanase and cellulase positive colonies were analysed by observing the zone of substrate (wheat bran and waste paper) hydrolysis around the colonies. A total of 30 bacterial isolates were obtained from termite gut and termitarium, respectively. Xylan and cellulose degrading potential of the positive isolates was also quantitatively estimated using agro-wastes-based medium. All the bacterial isolates displayed cellulase and xylanase activities in the range of 0.45-6.80 and 51-380 IU/ml, respectively. This is the first report mentioning the isolation of xylano-cellulolytic microbes from termite gut and termitarium using very simple cost-effective methodology.

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Production of Lignocellulolytic Enzymes by Microorganisms Isolated from Bulbitermes sp. Termite Gut in Solid-State Fermentation

Cited by 31 publications

References 63 publications

Exoproduction and Molecular Characterization of Peroxidase from Ensifer adhaerens

Exoproduction and Molecular Characterization of Peroxidase from Ensifer adhaerens

Agrowastes utilization by Raoultella ornithinolytica for optimal extracellular peroxidase activity

Cost-effective screening and isolation of xylano-cellulolytic positive microbes from termite gut and termitarium

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