A Bradford multiplexing method for protein estimation in fermented foods: Soy sauces

Shukla̽, Shruti

doi:10.3329/bjp.v11i1.25796

Cited by 7 publications

(4 citation statements)

References 3 publications

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“…This method is based on the binding of the Coomassie Brilliant Blue to the protein. Consequently, the amount of blue color produced from protein binding to Coomassie Brilliant Blue reagent is measured at 595 nm which is proportional to the concentration of the protein solution 27,28 . To prepare the Bradford solution, 0.01 g of Coomassie Brilliant Blue G‐250 was dissolved in 5 ml of 95% ethanol.…”

Section: Methodsmentioning

confidence: 99%

“…Consequently, the amount of blue color produced from protein binding to Coomassie Brilliant Blue reagent is measured at 595 nm which is proportional to the concentration of the protein solution. 27,28 To prepare the Bradford solution, 0.01 g of Coomassie Brilliant Blue G-250 was dissolved in 5 ml of 95% ethanol. Then, 10 ml phosphoric acid 85% was added, followed by the addition of distilled water up to 100 ml total volume.…”

Section: Determination Of Protein Levelmentioning

confidence: 99%

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Immobilization of urease enzyme on chitosan/polyvinyl alcohol electrospun nanofibers

Amani

Taghavi

Yazdian

et al. 2022

Biotechnology Progress

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Electrospun nanofibers have gained much attention for enzyme immobilization due to their high surface‐to‐volume ratio. In this study, urease was immobilized on chitosan/poly(vinyl alcohol) (PVA) nanofibers by both adsorption and crosslinking methods. In order to obtain nanofibers with more desirable properties, solutions with different ratios of chitosan and PVA were electrospun and crosslinked using glutaraldehyde. Comparing SEM images of the nanofibers, before and after immersing them in phosphate buffer, it was shown that higher chitosan content leads to more stable fibers. So, the solution with the chitosan to PVA ratio of 40:60 was used for enzyme immobilization. Then, the effects of initial protein concentration, temperature, incubation time, and method of immobilization were investigated to reach the highest enzyme activity. Under similar immobilization conditions, covalently immobilized urease showed higher activity, compared to uncrosslinked immobilized enzyme. Besides, it retained 30% of its initial activity after 10 times usage. So, this method was chosen for further investigation. Not only the activity of the immobilized enzyme was much higher than the free enzyme in a wide range of pH and temperature, but also stability of the immobilized enzyme was improved. Immobilized urease was then used to remove thiourea which is a toxic compound. Findings indicated 60% hydrolysis of initial thiourea in 12 h. In conclusion, the findings showed that chitosan/PVA nanofibers are suitable candidates for the immobilization of urease.

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Section: Methodsmentioning

confidence: 99%

Section: Determination Of Protein Levelmentioning

confidence: 99%

Immobilization of urease enzyme on chitosan/polyvinyl alcohol electrospun nanofibers

Amani

Taghavi

Yazdian

et al. 2022

Biotechnology Progress

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“…The microsomal pellets were resuspended in 100 mM PBS (pH 7.4) containing 20% glycerol and stored frozen at −80°C until analysis 22 . The amount of microsomal protein was determined following the method of Bradford 23 using BSA as a standard. The microsomal protein concentration was 17.881 mg/mL in the type 2 diabetic rats and 14.431 mg/mL in the normal rats.…”

Section: Methodsmentioning

confidence: 99%

Metabolic study of ginsenoside Rg3 and glimepiride in type 2 diabetic rats by liquid chromatography coupled with quadrupole‐Orbitrap mass spectrometry

Yang

et al. 2021

Rapid Comm Mass Spectrometry

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Rationale Ginsenoside Rg3 and glimepiride have been applied to treat type 2 diabetes (T2DM) because of their good hypoglycemic effects. In this study, the effects of ginsenoside Rg3 acting synergistically with glimepiride were investigated in liver microsomes from rats with type 2 diabetes. Methods An in vitro incubation system with normal rat liver microsomes (RLM) and type 2 diabetic rat liver microsomes (TRLM) was developed. The system also included two experimental groups consisting of RLM and TRLM pretreated with ginsenoside Rg3 and glimepiride (named the RLMR and TRLMR groups, respectively). The metabolism in the different groups was analyzed by ultra‐performance liquid chromatography coupled with quadrupole‐orbitrap mass spectrometry (UPLC/Q‐Orbitrap MS). Results The results showed that the concentration of glimepiride increased in RLM and TRLM after treatment with ginsenoside Rg3. Five metabolites (M1–M5) of glimepiride were found, and they were named 3N‐hydroxyglimepiride, hydroxyglimepiride, 1,2‐epoxy ether‐3‐hydroxyglimepiride, 1N‐hydroxyglimepiride and 1N,2C,S,O,O‐epoxy ether‐3‐hydroxyglimepiride. The metabolite of ginsenoside Rg3 was ginsenoside Rh2. Conclusions An in vitro incubation system with RLM and TRLM was developed. The system revealed pathways that produce glimepiride metabolites. Ginsenoside Rg3 may inhibit the activity of cytochrome P450 enzymes in vitro. The present study showed that ginsenoside Rg3 and glimepiride may be combined for the treatment of T2DM.

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“…The sample was mixed well, allowed to react for 1 min, and processed for cell counting using a counting Neubauer's chamber. The method reported earlier in the literature (Shukla. 2015) was used for the protein analysis of the samples.…”

Section: Measurement Of Residual Sugar and Intracellular Protein Conc...mentioning

confidence: 99%

Strain improvement for enhanced erythritol production by Moniliella pollinis Mutant-58 using jaggery as a cost-effective substrate

Khatape,

Rangaswamy,

Dastager

2023

Int Microbiol

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Erythritol has been produced by various microorganisms including Yarrowia, Moniliella, Aureobasidium, and Candida strains. Due to its relatively high price erythritol sweetener used lesser than other polyols despite having many advantages. Therefore, in this study, Moniliella pollinis strain was improved for erythritol production by chemical mutagenesis and subsequently screening for cost-effective carbon sources for the enhanced erythritol yield. M. pollinis was subjected to N-methyl N-nitro N-nitroso guanidine (NTG), Ethyl methyl sulphonate (EMS), and UV mutagenesis for improved erythritol production. The mutant strains were evaluated for enhanced erythritol production medium optimization by using different carbon substrates at the shake ask level. To enhance the production of erythritol and statistical media optimization was carried out using a central composite design (CCD). Among 198 isolated mutants, Mutant-58 strain generated by EMS mutagenesis was selected for further assessment. The Mutant-58 strain showed signi cant morphological changes as compared to the parent strain. Furthermore, statistically optimized media composition resulted in the higher production of erythritol (91.2±3.4 g/L) with a yield of 40.7±3.4 % in shake ask experiments. The optimized medium composition for erythritol production constitutes (g/L) 225 jaggery, 4.4 yeast extract (YE), 4.4 KH 2 PO 4 , 0.31 MgSO 4, and pH 5.5. The present study demonstrated strain improvement, media, and process optimization resulting in a 30% increase in the erythritol production in the Mutant-58 as compared to the parent strain. This is also the rst instance where jaggery has been used as a cost-effective carbon source alternative to glucose for industrial-scale erythritol production.

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A Bradford multiplexing method for protein estimation in fermented foods: Soy sauces

Cited by 7 publications

References 3 publications

Immobilization of urease enzyme on chitosan/polyvinyl alcohol electrospun nanofibers

Immobilization of urease enzyme on chitosan/polyvinyl alcohol electrospun nanofibers

Metabolic study of ginsenoside Rg3 and glimepiride in type 2 diabetic rats by liquid chromatography coupled with quadrupole‐Orbitrap mass spectrometry

Strain improvement for enhanced erythritol production by Moniliella pollinis Mutant-58 using jaggery as a cost-effective substrate

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