Isolation and characterization of protease producing bacteria from upper respiratory tract of wild chicken

Raut, Sangeeta; Sen, Sudip Kumar; Kabir, Naveed Alam; Satpathy, Soumya; Raut, Smita

doi:10.6026/97320630008326

Cited by 10 publications

(5 citation statements)

References 12 publications

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“…Effect of pH on enzyme production was determined by adjusting pH of basal medium from 5 to 12, using Na 2 HPO 4 -NaH 2 PO 4 buffer solution (pH [5][6][7][8] and NaHCO 3 -NaOH buffer solution (pH [9][10][11][12].…”

Section: Determination Of Optimum Growth Conditionsmentioning

confidence: 99%

“…Microbial proteases represent $40% of all the industrial enzyme sales throughout the world 7 . Microbial proteases consist of acidic, neutral and alkaline enzymes; furthermore, depending on the characteristics of the active site group, metallo, aspartic, cysteine and serine types may occur 7,8 . Alkaline proteases, physiologically and commercially important catalysts, are active in a neutral to alkaline pH range, holding 450% of the total enzyme market 9 .…”

Section: Introductionmentioning

confidence: 99%

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Production of an alkaline protease using Bacillus pumilus D3 without inactivation by SDS, its characterization and purification

Özçelik

Aytar

Gedikli

et al. 2013

Journal of Enzyme Inhibition and Medicinal Chemistry

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In this study, protease-producing capacity of Bacillus pumilus D3, isolated from hydrocarbon contaminated soil, was evaluated and optimized. Optimum growing conditions for B. pumilus D3 in terms of protease production were determined as 1% optimum inoculum size, 35 C temperature, 11 pH and 48 h incubation time, respectively. Stability studies indicated that the mentioned protease was stable within the pH range of 7-10.5 and between 30 C and 40 C temperatures. Surprisingly, the activity of the enzyme increased in the presence of SDS with concentration up to 5 mM. The protease was concentrated 1.6-fold with ammonium sulfate precipitation and dialysis. At least six protein bands were obtained from dialysate by electrophoresis. Four clear protein bands with caseinolytic activity were detected by zymography. Dialysate was further purified by anion-exchange chromatography and the caseinolytic active fraction showed a single band between 29 and 36 kDa of reducing conditions.

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Section: Determination Of Optimum Growth Conditionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Production of an alkaline protease using Bacillus pumilus D3 without inactivation by SDS, its characterization and purification

Özçelik

Aytar

Gedikli

et al. 2013

Journal of Enzyme Inhibition and Medicinal Chemistry

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show abstract

“…The mixture was incubated at room temperature for 1 h. After incubation, the reaction mixture was centrifuged at 12,000× g for 5 min, and the absorbance of the supernatant was measured at 280 nm. One unit of protease is defined as the amount of enzyme that hydrolyzes casein to produce equivalent absorbance to 1 µmol of tyrosine/min with tyrosine as standard [ 47 ].…”

Section: Methodsmentioning

confidence: 99%

Enzyme Production and Inhibitory Potential of Pseudomonas aeruginosa: Contrasting Clinical and Environmental Isolates

Aqel,

Sannan,

Foudah

et al. 2023

Antibiotics

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(1) Background: This study summarizes the findings of two studies investigating the inhibitory effects of Pseudomonas aeruginosa strains from clinical and environmental sources against gram-positive and gram-negative bacteria and fungi. The studies also analyzed the correlation between enzyme production and inhibitory effects to gain insights into the antimicrobial capabilities of P. aeruginosa strains; (2) Methods: Both studies employed similar methodologies, including the use of disk diffusion and well diffusion methods to assess the inhibitory effects of P. aeruginosa strains against target pathogens. Enzyme production was analyzed through various biochemical assays to determine the diversity and frequencies of enzyme secretion among the strains; (3) Results: A comparative analysis of enzyme production in P. aeruginosa strains from clinical sources revealed significant variations in enzyme production, with hemolysin and protease being the most commonly produced enzymes. Gelatinase production showed lower rates, whereas chondroitinase and hyaluronidase were absent or occurred less frequently. In contrast, a comparative analysis of enzyme production in environmental isolates showed different patterns, indicating adaptation to environmental conditions. Pyocyanin production was absent in all environmental isolates. The inhibitory effects against gram-positive and gram-negative bacteria varied among different P. aeruginosa strains, with strain-specific variations observed. Limited inhibitory effects were observed against fungi, primarily toward gram-positive bacteria; (4) Conclusions: The findings highlight the strain-specific nature of inhibitory effects and enzyme production in P. aeruginosa strains. The correlation between enzyme production and inhibitory effects against gram-positive bacteria suggest a potential role of specific enzymes, such as hemolysin and protease, in the antimicrobial activity. The complexity of the relationship between enzyme production and the inhibition of different pathogens requires further investigation. The results emphasize the potential of P. aeruginosa strains as sources for antimicrobial strategies, particularly against gram-positive bacteria. Future research should focus on understanding the mechanisms underlying these inhibitory effects and exploring their therapeutic applications.

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“…The clear zone formed around the colony was due to the ability of bacterial protease to degrade the casein substrate contained in the skim milk agar media. Casein is hydrolyzed by bacterial protease to produce soluble peptides and amino acids [36,37]. hydrolysis activity of bacterial protease could be measured by calculating the ratio between the diameter of the clear zone around the bacterial colony and the diameter of the bacterial colony [38].…”

Section: Proteolytic Testmentioning

confidence: 99%

Optimization of Crude Protease Production from Bacillus thuringiensis HSFI-12 and Thrombolytic Activity Its Enzyme Dialysate

Zafrida

Ethica²,

Ernanto³

et al. 2022

Trends Sci

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Cardiovascular disease (CVD) is among the leading causes of death in the world caused by thrombosis. Thrombosis is the formation of excessive blood clots on the walls of blood vessels called thrombus. This could lead to fatal blockage of the heart muscle or brain. Thrombosis can be treated using enzyme-type drugs such as thrombolytic proteases. There have been many studies of bacteria producing thrombolytic enzymes isolated from fermented foodstuffs. However, commercial production of bacterial enzymes to fulfill the need of thrombolytic agents is still limited, causing high price of CVD therapy. Bacillus sp. HSFI-12 (Holothuria scabra Fermented Intestine-12) isolated from the fermented intestine of sea cucumber Holothuria scabra had been reported to have a competitive thrombolytic activity to the commercial Nattokinase. This study aimed to determine bacterial optimum incubation time based on enzyme activity after bacterium molecular identification was done. It also aimed to obtain the dialysate of bacterial crude protease and then determine the thrombolytic activity of the obtained dialysate. Thrombolytic activity was tested on 4 different types of blood (A, B, AB and O). Results of molecular identification showed that strain HSFI-12 shared similarity level of 99.80 %, with Bacillus thuringiensis. Activity of crude protease from the incubated cultures peaked at 48 h of incubation with activity of 191.5 U/mL The activity of concentrated protease after precipitation and dialysis process (dialysate) was 2-times higher by 355,7 U/mL. The percentage of lysis of blood clots produced by crude blood groups A, B, AB and O showed a range of values of 66.423 - 67.656 % while those that produce dialysate are 77.564 - 78.861 %. As conclusion, the best (optimized) incubation time to produce crude enzyme from B. thuringiensis HSFI-12 with the highest activity was 48 h. The process of concentrating the crude thrombolytic protease of B. thuringiensis HSFI-12 increases both activity and thrombolytic ability of the bacterial enzyme. HIGHLIGHTS The most optimum incubation time for protease production from Bacillus thuringiensis is 48 h Partial purification on bacterial crude protease through resulted in 86 % increased activity Partial purification on bacterial crude protease resulted in 17 % increased blood clot lysis ability Clot lysis ability of both crude and dialysate proteases are higher than that of Nattokinase (NK) GRAPHICAL ABSTRACT

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Isolation and characterization of protease producing bacteria from upper respiratory tract of wild chicken

Cited by 10 publications

References 12 publications

Production of an alkaline protease using Bacillus pumilus D3 without inactivation by SDS, its characterization and purification

Production of an alkaline protease using Bacillus pumilus D3 without inactivation by SDS, its characterization and purification

Enzyme Production and Inhibitory Potential of Pseudomonas aeruginosa: Contrasting Clinical and Environmental Isolates

Optimization of Crude Protease Production from Bacillus thuringiensis HSFI-12 and Thrombolytic Activity Its Enzyme Dialysate

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