Optimization of Protease Production by Bacillus isronensis Strain KD3 Isolaed from Dairy Industry Effluent

Patil, N. S.; Kurhekar, Jaya Vikas

doi:10.46488/nept.2020.v19i03.041

Cited by 4 publications

(5 citation statements)

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“…A closer agitation speed of 155 rpm was reported to enhance protease activity by Bacillus subtilis IMRUZ -7 [34] while Niyomukiza et al [27] reported that better protease activity was achieved at 180 rpm. In another study, a higher agitation speed of 200 rpm (49±0.058 U/mL) enhanced the protease synthesis of Bacillus isronensis strain KD3 while the second best was attained at 150 rpm (26 ±0.32 U/mL) [35].…”

Section: Agitation Ratesmentioning

confidence: 94%

“…Contrarily, supplementing the production medium with nitrogen sources like malt extract, tryptone, ammonium sulphate, and beef extract did not have any effect on protease production by Bacillus isronensis strain KD3 [35]. The utilization of nitrogen sources by microorganisms is species-specific due to their genetic differences, which could have contributed to the variation.…”

Section: Nitrogen Sourcesmentioning

confidence: 96%

“…mar64, Bacillus strain, Bacillus subtilis, and Bacillus subtilis PTCC1254, respectively. In an investigation carried out by Patil and Kurhekar [35], the effects of carbon sources such as maltose, sucrose, glucose, and starch on protease production were tested. The researchers observed that the carbon sources had no positive effect on protease production by Bacillus isronensis strain KD3 isolated from dairy industrial effluent.…”

Section: Carbon Sourcesmentioning

confidence: 99%

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Molecular Characterization and Optimization of Alkaline Protease Production by Bacillus cereus LS23B

Ogunniran,

Ohunayo,

Daramola

et al. 2023

AJB2T

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The study aimed to determine the conditions leading to maximum protease production using submerged fermentation and detecting the presence of protease genes in the bacteria. This is necessary to meet the increasing demand for protease enzymes in the industrial market. The ability of the bacterial isolate to produce protease enzymes was evaluated through primary screening. After that, morphological characterization, biochemical tests, and 16S rRNA analysis were done to identify the bacterial strain. To confirm the presence of the gene-encoding enzyme, the protease (npr) gene primer was amplified using a polymerase chain reaction. The pH, incubation duration, temperature, carbon, and nitrogen sources were studied. Others include metal ions, substrate concentration, and agitation speed. The bacterial strain has 100% similarity to Bacillus cereus A9, while the protease encoding gene was confirmed with positive bands of 951bp. The enzyme was optimally produced at 40 oC with a pH of 9 after 72 h incubation. Starch, gelatin, 1 % substrate concentration, 1mM K+, and agitation speed of 160 rpm fully supported protease production. The presence of the npr gene in the isolate was confirmed. Also, the optimization study reveals that Bacillus cereus LS23B can be used in large-scale protease production, which may be used in different biotechnological applications.

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Section: Agitation Ratesmentioning

confidence: 94%

Section: Nitrogen Sourcesmentioning

confidence: 96%

Section: Carbon Sourcesmentioning

confidence: 99%

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Molecular Characterization and Optimization of Alkaline Protease Production by Bacillus cereus LS23B

Ogunniran,

Ohunayo,

Daramola

et al. 2023

AJB2T

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“…Based on the data in Table 6., an agitation speed of 150 rpm resulted in the highest enzyme activity of 106.39 ± 9.30 U/mL, but at an agitation speed of 100 and 200 rpm the enzyme activity decreased by 68.72% and 78, 63%. In the study of Patil and Kurhekar (2020), protease activity by Bacillus isronensis increased at an agitation speed of 100-200 rpm, but decreased at an agitation speed of 250 rpm [27]. Agitation can play a role in helping to homogenize the mixture in the media [49].…”

Section: Table 6 Table Of the Effect Of Enzyme Activity On Variations...mentioning

confidence: 99%

Screening of Factors Influencing Keratinase Fermentation from Bacillus Haynesii BK1H using The Plackett-Burman Design (PBD)

Firli Masruroh,

Hendrik Sanjaya,

Alvionita

et al. 2024

E3S Web Conf.

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Keratinase is a class of proteases that degrade keratin into polypeptides and amino acids by breaking peptide and disulfide bonds in keratinous proteins. Protease is one of the largest industrial enzymes, the global protease market is increasing rapidly every year. In previous studies, a keratinase-producing microbe was isolated from Bleduk Kuwu which was identified as Bacillus haynesii BK1H. However, further study needs to be done to optimize the production by observing microenvironmental factors that influence keratinase production. In this study, screening some microenvironmental factors is reported. Screening factors including carbon sources, type and concentration of metal ions, agitation speed, amount of inoculum, pH, and temperature. Screening for these factors was started with the One Factor at A Time (OFAT) method and followed by the Plackett-Burman Design (PBD) method. In this study, sequential work was done: (1) Regeneration of Bacillus haynesii BK1H Microbes, (2) Preparation of Tyrosine Standard Series Solutions, (3) Screening of Factors Affecting Protease Fermentation of Bacillus haynesii BK1H using the One Factor at A Time (OFAT) method. ), and (4) Maintaining Significantly Influential Factors by Using Plackett-Burman Design (PBD). The results of the OFAT approach showed that the best condition for keratinase production was achieved at rice husk concentration, additional carbon source, of 1%; pH of 7; a temperature of 35°C; the amount of inoculum of 1%; agitation speed of 150 rpm; magnesium sulfate concentration of 0.04 g/mL, and calcium chloride concentration of 0.0005 g/m. Justification of those factors using PBD confirmed that only additional rice husk, magnesium sulfate and calcium chloride concentration, and agitation speed were significantly important toward keratinase production at selected experiment level limits.

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“…Whereas, protease of Geobacillus thermoglucosidasius SKF4 exhibit maximum protease activity at pH 7 to 8 (Suleiman et al, 2020) [18] . Bacillus isronensis strain KD3 produced maximum proteases at 42°C and pH 7-8 after 48h of the incubation period (Patil and Kurhekar, 2020) [19] . Alkaline protease of Bacillus sp.…”

Section: Effect Of Ph On Protease Activitymentioning

confidence: 99%

Novel alkaline protease of <em>Staphylococcus cohnii </em>N3 isolated from poultry farm soil used for silver recovery from waste X-ray film

Radhathirumalaiarasu¹,

Taj²

2021

Int. J. Appl. Res.

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Alkaline proteases are one of the most widely used as industrial enzyme recently explored for its effective degrading ability in bioremediation. In the present study alkaline protease producing bacteria was isolated from soil samples collected from waste dumped area in poultry farm. The isolate was identified as Staphylococcus cohnii N3 strain by 16s rRNA sequencing analysis. The effect of pH and temperature on alkaline protease was found that showed maximum activity at pH 9 and at temperature 60 ℃ (162.U/ml). The isolated S. cohnii N3 was further experimented for silver recovery and gelatin hydrolysis. Gelatin hydrolysis was monitored by measuring increase in turbidity in the hydrolysate. Gelatin layer was stripped completely within 20 min at 40 ˚C, pH 9. Rate of gelatin hydrolysis increased with increased in time shows complete decolorization of X-ray film proves its suitability for silver recovery.

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Optimization of Protease Production by Bacillus isronensis Strain KD3 Isolaed from Dairy Industry Effluent

Cited by 4 publications

References 0 publications

Molecular Characterization and Optimization of Alkaline Protease Production by Bacillus cereus LS23B

Molecular Characterization and Optimization of Alkaline Protease Production by Bacillus cereus LS23B

Screening of Factors Influencing Keratinase Fermentation from Bacillus Haynesii BK1H using The Plackett-Burman Design (PBD)

Novel alkaline protease of <em>Staphylococcus cohnii </em>N3 isolated from poultry farm soil used for silver recovery from waste X-ray film

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