Identification and characterization of a calcium dependent bacillopeptidase from Bacillus subtilis CFR5 with novel kunitz trypsin inhibitor degradation activity

Sharmila, G.R.; Halami, Prakash M.; Venkateswaran, G.

doi:10.1016/j.foodres.2017.10.049

Cited by 7 publications

(3 citation statements)

References 36 publications

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“…However, soy and other leguminous plants contain antinutritional factors, such as trypsin inhibitors, lectins, and toxic oligosaccharides, with capacity to produce tissue damage and animal death. In this sense, some Bacillus species have been reported with the capacity to break down antinutritional factors contained in soy products ( Shi et al, 2017 ; Giliyaru et al, 2018 ).…”

Section: Discussionmentioning

confidence: 99%

Assessment of Bacillus species capacity to protect Nile tilapia from A. hydrophila infection and improve growth performance

Macias,

Mercado,

Olmos

2024

Front. Cell. Infect. Microbiol.

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The present study evaluated the capacity of three Bacillus species to improve health status and growth performance of Nile Tilapia fed with high levels of soybean meal and challenged with Aeromonas hydrophila. In vitro experiments showed that β-hemolysin and metalloprotease enzymes were produced by A. hydrophila throughout the exponential growth phase. In vivo experiments showed that 107 colony-forming units (CFUs)/ml of this pathogen killed 50% of control group fishes in 13 days. To evaluate the influence of Bacillus strains on health status and growth performance in Nile Tilapia, 180 fishes (33.44 + 0.05 g) were distributed in 12 tanks of 200 L each, and animals were fed twice per day until satiety. 1) Control group without Bacillus, 2) Bacillus sp1, 3) Bacillus sp2, and 4) Bacillus sp3 groups were formulated containing 106 CFU/g. After 40 days of feeding, the fishes were intraperitoneally injected with 1 ml of A. hydrophila at 2 × 107 CFU/ml, and mortality was recorded. The results showed that cumulative mortality rate was significantly (p< 0.05) lower in the Bacillus sp1 (25%), sp2 (5%), and sp3 (15%) groups, than the control group (50%). Weight gain was also significantly better (p< 0.05) in the Bacillus sp1 (36%), sp2 (67%), and sp3 (55%) groups with respect to the control group (30%). In conclusion, functional diet formulated with high levels of soybean meal and supplemented with Bacillus sp2 could be an alternative to protect Nile tilapia cultures from A. hydrophila infections and improve fish growth performance.

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Section: Discussionmentioning

confidence: 99%

Assessment of Bacillus species capacity to protect Nile tilapia from A. hydrophila infection and improve growth performance

Macias,

Mercado,

Olmos

2024

Front. Cell. Infect. Microbiol.

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“…Furthermore, the peptidase activity of PPPase was almost wholly inactivated in the presence of 5 mM Fe +3 . Bankus & Bond (2001) (Sharmila et al 2018) in the presence of Ca +2 ions. It has been reported that Ca +2 ions stabilize thermolysin by preventing autolysis (Wu & Chen 2011).…”

Section: Effect Of Metal Ions On Enzyme Activitymentioning

confidence: 99%

“…Crude enzyme solution (CES)Partially purified peptidase (PPPase)b)An extracellular metallopeptidase produced by Bacillus amyloliquefaciens FE-K155Trakya Univ J Nat Sci, 21(1):[47][48][49][50][51][52][53][54][55][56][57][58][59][60][61] 2020 Peptidase activity results at different temperatures.…”

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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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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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Trends in extracellular serine proteases of bacteria as detergent bioadditive: alternate and environmental friendly tool for detergent industry

Salwan

Sharma

2019

Arch Microbiol

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Identification and characterization of a calcium dependent bacillopeptidase from Bacillus subtilis CFR5 with novel kunitz trypsin inhibitor degradation activity

Cited by 7 publications

References 36 publications

Assessment of Bacillus species capacity to protect Nile tilapia from A. hydrophila infection and improve growth performance

Assessment of Bacillus species capacity to protect Nile tilapia from A. hydrophila infection and improve growth performance

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

Trends in extracellular serine proteases of bacteria as detergent bioadditive: alternate and environmental friendly tool for detergent industry

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