Protease obtention using Bacillus subtilis 3411 and amaranth seed meal medium at different aeration rates

Pastor, M. D.; Lorda, Graciela Susana; Balatti, A P

doi:10.1590/s1517-83822001000100002

Cited by 43 publications

(31 citation statements)

References 6 publications

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“…K-30 (25,28) respectively. This indicates that MBRI 7 (present work) exhibited maximum protease activity in lesser fermentation time which is a major prerequisite for commercial production.…”

Section: Resultsmentioning

confidence: 99%

Characterization of novel extracellular protease produced by marine bacterial isolate from the Indian Ocean

Fulzele¹,

DeSa²,

Yadav³

et al. 2011

Braz. J. Microbiol.

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Out of the vast pool of enzymes, proteolytic enzymes from microorganisms are the most widely used in different industries such as detergent, food, peptide production etc. Several marine microorganisms are known to produce proteases with commercially desirable characteristics. We have isolated nine different cultures from marine samples of the Indian Ocean. All of them were i) motile ii) rod shaped iii) non spore forming iv) catalase and amylase positive v) able to grow in presence of 10 % NaCl. They produced acid from glucose, fructose and maltose and grew optimally at 30 0 C temperature and pH 7.0-8.0. None of them could grow above 45 0 C and below 15 0 C. Only one of them (MBRI 7) exhibited extracellular protease activity on skim milk agar plates. Based on 16S rDNA sequencing, it belonged to the genus Marinobacter (98% sequence similarity, 1201 bp). The cell free extract was used to study effects of temperature and pH on protease activity. The optimum temperature and pH for activity were found to be 40 0 C and 7.0 respectively. The crude enzyme was stable at temperature range of 30-80 0 C and pH 5.0-9.0. It retained 60 % activity at 80 0 C after 4 h and more than 70 % activity at 70 0 C after 1 h. D value was found to be 342 minutes and 78 minutes for 40 0 C and 80 0 C respectively. Interestingly the enzyme remained 50 % active at pH 9.0 after 1 h. Comparison with other proteases from different microbial sources indicated that the neutral protease from the halotolerant marine isolate MBRI 7 is a novel enzyme with high thermostability.

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Section: Resultsmentioning

confidence: 99%

Characterization of novel extracellular protease produced by marine bacterial isolate from the Indian Ocean

Fulzele¹,

DeSa²,

Yadav³

et al. 2011

Braz. J. Microbiol.

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“…Proteases are highly exploited enzymes in food, leather, detergent, pharmaceutical, diagnostics, waste management and silver recovery (Babu and Lakshmi, 2005). Bacillus protease is of special importance because of its wide applications in various industries like pharmaceutical, leather, food and waste processing industries (Pastor et al, 2001). The GC content of the isolate was also found to be relatively high.…”

Section: Discussionmentioning

confidence: 99%

Enzymatic Screening and Molecular Characterization of Thermophilic Bacterial Strains Isolated from Hotspring of Tatopani, Bhurung, Nepal

Adhikari

Ghimire

Khatri

et al. 2015

Int J Appl Sci Biotechnol

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Background and Aim: In Nepal not much of study of Thermophilic area and Thermophiles have been done. Thermophilic bacteria are less studied but are important group of microorganisms due to their ability to produce industrially important enzymes. Methods: In this study, thermophilic bacteria were isolated from hot spring of Bhurung, Nepal. Wide range of bacteria that could grow at high temperatures and tolerate extreme temperature were characterized by morphology, biochemistry and sequencing of its 16S rRNA gene sequence. The isolates were screened for production of extracellular enzymes like protease, amylase, lipase, cellulase, caseinase, pectinase and xylanase activity. Phylogenetic tree construction and G+C content evaluation of the isolate was also studied.Results: 15 isolates with ability to tolerate high temperatures were identified as Bacillus sp. by morphology, biochemistry and sequencing of its 16S rRNA gene sequence. BLAST search analysis of the sequence was performed and result showed maximum identity (99% similarity) with Bacillus licheniformis, Bacillus subtilis and Bacillus pumilus. Isolated strains exhibited considerable amount of extracellular exozymes activity. Phylogenetic analysis of the isolates revealed the relatedness among the species. The G+C content of each species was also evaluated and was found to be in range of 54.87 to 55.54%.Conclusion: The study of isolates confirmed that the isolated Bacillus sp. to be a true thermophile and could be a source of various thermostable exozymes which can be exploited for pharmaceutical and industrials applications. Much detailed study of the isolates can Int J Appl Sci Biotechnol, Vol 3(3): 392-397

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“…Proteases have a variety of applications in detergent, pharmaceutical, leather, and food industries [1][2][3]. Globally, proteases constitute the largest product segment of industrial enzymes, accounting for about 60% of the total worldwide enzyme sales [4,5].…”

Section: Introductionmentioning

confidence: 99%

Purification and partial characterization of serine alkaline metalloprotease from Bacillus brevis MWB-01

Olajuyigbe

Falade

2014

Bioresour. Bioprocess.

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Background: Proteases from bacteria are among the most important hydrolytic enzymes that have been studied due to their extracellular nature and high yield of production. Of these, alkaline proteases have potential for application in detergent, leather, food, and pharmaceutical industries. However, their usefulness in industry is limited by low activity and stability at high temperatures, extreme pH, presence of organic solvents and detergent ingredients. It is therefore very crucial to search for new alkaline proteases with novel properties from a variety of microbial sources. Results: In the present study, 21 Bacillus species isolated from organic waste sites were screened for proteolytic activity on casein agar. Bacillus brevis MWB-01 exhibited highest proteolytic activity with a clear zone diameter of 35 mm. Production of protease from B. brevis MWB-01 was investigated in optimized media after 48 h of cultivation with shaking (180 rpm) at 37°C. The protease was partially purified in a two-step procedure using ammonium sulphate precipitation and gel filtration chromatography on Sephadex G-200 column. The enzyme was purified 2.1-fold with yield of 4.6%. The purified protease had optimum temperature of 40°C with relative activity of about 50% at 50°C and was uniquely stable up to 60°C after 30 min of incubation exhibiting 63% residual activity. The enzyme had optimum pH of 8.0 and remarkably showed relative activity above 70% at pH 9.0 to 11.0 and 53% at pH 12.0, respectively and was very stable over a wide pH range (6.0 to 12.0). Ca 2+ and Mn 2+ increased protease activity with 9.8% and 3.5%, respectively; Hg 2+ and Zn 2+ strongly inhibited protease activity by 89% and 86%. The almost complete inhibition of the enzyme by phenylmethylsulphonyl fluoride (PMSF) and ethylene diamine tetra acetic acid (EDTA) confirmed the enzyme as a serine metalloprotease. The enzyme had highest compatibility with Sunlight, a commercial laundry detergent.

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Protease obtention using Bacillus subtilis 3411 and amaranth seed meal medium at different aeration rates

Cited by 43 publications

References 6 publications

Characterization of novel extracellular protease produced by marine bacterial isolate from the Indian Ocean

Characterization of novel extracellular protease produced by marine bacterial isolate from the Indian Ocean

Enzymatic Screening and Molecular Characterization of Thermophilic Bacterial Strains Isolated from Hotspring of Tatopani, Bhurung, Nepal

Purification and partial characterization of serine alkaline metalloprotease from Bacillus brevis MWB-01

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