Investigation on Production and Purification of Haloalkalophilic Organic Solvent Tolerant Protease from Marine Shell Waste and its Bioconversion to Chitin by Aquatic Bacillus sp. APCMST-CS4

Maruthiah, Thirumalai; Somanath, Beena; Immanuel, G.; Palavesam, A.

doi:10.1007/s12649-016-9636-8

Cited by 7 publications

(2 citation statements)

References 38 publications

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“…TKU004 CES remaining after incubation at 4 and 25°C for 10 days was 65 %. In another study, it was shown that the activity decreased by 21 % and increased by 31 % with acetone and ethanol, respectively (Maruthiah et al 2017). Bacillus sp.…”

Section: Effect Of Some Organic Solvents and Surfactants On Peptidase Activitymentioning

confidence: 95%

“…The results obtained are comparable to those of Manni et al (2008) who also reported that 60 % of metallopeptidase activity remained after incubation at 50°C for 1 h, and of Sousa et al (2007) who found 55 % activity remaining at the same temperature after 2 h of incubation. Maruthiah et al (2017) reported that a more than 80 % activity of their serine metallopeptidase remained after 1.3 h of incubation within the temperature range between 40 and 60°C. Furhan et al (2019) observed that more than half of the activity of cold-active metallopeptidase was retained between 20-30°C.…”

Section: Optimum Temperature Of Peptidase and Temperature Stabilitymentioning

confidence: 99%

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PARTIAL PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR METALLOPEPTIDASE PRODUCED BY Bacillus amyloliquefaciens FE-K1

Erem

İnan

Budak

et al. 2020

Trakya University Journal of Natural Sciences

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The aim of this study was to purify and characterize the peptidase of Bacillus amyloliquefaciens (Fukumoto) (strain FE-K1) isolated from ropey bread. Peptidases were purified from crude enzyme solution by affinity chromatography with an efficiency of 25 % and a purification coefficient of 1.53. The optimum pH of partially purified peptidase (PPPase) solution was determined as 7.5 and the peptidases retained approximately 90 % of their initial activity in the pH range 7.0-8.5 following incubation at 37°C for 2 h. The optimum temperature for the PPPase was 60°C. The approximate molecular weight of the PPPase was determined as 36 kDa. Inactivation of the PPPase in the presence of O-FEN and EDTA showed them to be metallopeptidases and 5 mM of K +1 and 5 mM of Mn +2 ions increased the enzyme activity by 4 % and 6.15 %, respectively. The presence of Hg +2 , Fe +3 and SDS (0.1-1.0 % w/v) caused inactivation whereas the enzyme retained most of its activity in the presence of 0.1-1.0 % (v/v) Triton X-100, Tween 20 and Tween 80 and 1-20 % (v/v) xylene, ethanol, acetone and acetonitrile. Characterization of the PPPase revealed the enzyme as a neutral serine metallopeptidase compatible with some organic solvents and surfactants.Özet: Bu çalışmanın amacı, sünmüş ekmeklerden izole edilen Bacillus amyloliquefaciens (Fukumoto) (suş FE-K1) ile elde edilen peptidazı saflaştırmak ve karakterize etmektir. Peptidazlar ham enzim çözeltisinden afinite kromatografisi ile % 25 verim ve 1,53 saflaştırma katsayısı ile saflaştırılmıştır. Kısmi olarak saflaştırılmış peptidaz (PPPaz) çözeltisinin optimum pH değeri 7,5 olarak tespit edilmiş olup, pH 7,5-8,0 aralığında peptidaz, 37°C'de 2 saat inkübasyonun ardından başlangıç aktivitesini yaklaşık % 90 oranında korumuştur. PPPaz'ın optimum sıcaklığı 60°C'dir. PPPaz'ın yaklaşık molekül ağırlığı 36 kDa olarak belirlenmiştir. PPPaz'ın O-FEN ve EDTA varlığında inaktive olması, enzimin metallopeptidaz olduğunu göstermiştir. Ayrıca 5 mM K +1 ve 5 mM Mn +2 , enzimin aktivitesini sırasıyla % 4 ve % 6,15 oranında artırmıştır. Hg +2 , Fe +3 ve SDS (% 0,1-1,0 w/v) varlığı enzimin inaktivasyonuna neden olurken, % 0,1-1,0 (v/v) Triton X-100, Tween 20 ve Tween 80; ve % 1-20 (v/v) ksilen, etanol, aseton ve asetonitril varlığında enzim aktivitesini büyük ölçüde korumuştur. PPPaz'ın karakterizasyonu, enzimin bazı organik çözücü ve yüzey aktif maddelerle ile uyumlu nötr bir serin metalopeptidaz olduğunu ortaya çıkarmıştır.

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Section: Effect Of Some Organic Solvents and Surfactants On Peptidase Activitymentioning

confidence: 95%

Section: Optimum Temperature Of Peptidase and Temperature Stabilitymentioning

confidence: 99%

PARTIAL PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR METALLOPEPTIDASE PRODUCED BY Bacillus amyloliquefaciens FE-K1

Erem

İnan

Budak

et al. 2020

Trakya University Journal of Natural Sciences

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Response surface methodology for production, characterization and application of solvent, salt and alkali-tolerant alkaline protease from isolated fungal strain Aspergillus niger WA 2017

Wahab

Ahmed

2018

International Journal of Biological Macromolecules

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Marine microbial alkaline protease: An efficient and essential tool for various industrial applications

Barzkar

2020

International Journal of Biological Macromolecules

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Investigation on Production and Purification of Haloalkalophilic Organic Solvent Tolerant Protease from Marine Shell Waste and its Bioconversion to Chitin by Aquatic Bacillus sp. APCMST-CS4

Cited by 7 publications

References 38 publications

PARTIAL PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR METALLOPEPTIDASE PRODUCED BY Bacillus amyloliquefaciens FE-K1

PARTIAL PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR METALLOPEPTIDASE PRODUCED BY Bacillus amyloliquefaciens FE-K1

Response surface methodology for production, characterization and application of solvent, salt and alkali-tolerant alkaline protease from isolated fungal strain Aspergillus niger WA 2017

Marine microbial alkaline protease: An efficient and essential tool for various industrial applications

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