Semi Purification and Identifications Molecule Protein Weigh of Alkaline Protease Enzyme from Bacillus cereus LS2B

Junaidi, Yendri; Pertiwiningrum, Ambar; Erwanto, Yuny; Fitriyanto, Nanung Agus

doi:10.14257/ijbsbt.2017.9.3.08

Cited by 11 publications

(13 citation statements)

References 16 publications

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“…Amongst all tested buffers, relative activity of P1 protease fraction was the highest in 200 mM glycine-NaOH buffer (pH 10) as depicted in Figure 10. Dialysis causes diffusion of salt and nonprotein molecules diffuse into the solution (buffer) which has a lower pressure passing through the cellophane dialysis bag [75]. A consistent increase in purification fold and specific activity at each step was observed.…”

Section: Bulk Production and Partial Purification Of P1 Proteasementioning

confidence: 90%

Enhanced catalytic activity of Bacillus aryabhattai P1 protease by modulation with nanoactivator

Pathak

Rathod

Mahabole

et al. 2020

Heliyon

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In the developing area of modern nanobiotechnology, the research is being focused on enhancement of catalytic performance in terms of efficiency and stability of enzymes to fulfill the industrial demand. In the context of this interdisciplinary era, we isolated and identified alkaline protease producer Bacillus aryabhattai P1 by polyphasic approach and then followed one variable at a time approach to optimize protease production from P1. The modified components of fermentation medium (g/L) were wheat bran 10, soybean flour 10, yeast extract 5, NaCl 10, KH 2 PO 4 1, K 2 HPO 4 1 and MgSO 4 ⋅7H 2 O 0.2 (pH 9). The optimum alkaline protease production from P1 was recorded 75 AE 3 U/mg at 35 C and pH 9 after 96 h of fermentation period. Molecular weight of partially purified P1 alkaline protease was 26 KDa as revealed by SDS-PAGE. Calcium based nanoceramic material was prepared by wet chemical precipitation method and doped in native P1 protease for catalytic activity enhancement. Catalytic activity of modified P1 protease was attained by nanoactivator mediated modulation was more by 5.58 fold at pH 10 and 30 C temperature. The nanoceramic material named as nanoactivator, with grain size of 40-60 nm was suitable to redesign the active site of P1 protease. Such types of modified proteases can be used in different nanobiotechnological applications.

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Section: Bulk Production and Partial Purification Of P1 Proteasementioning

confidence: 90%

Enhanced catalytic activity of Bacillus aryabhattai P1 protease by modulation with nanoactivator

Pathak

Rathod

Mahabole

et al. 2020

Heliyon

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“…A study conducted in probiotics showed the three predominant protein molecules from the SDS-Page of Hi Trap ion exchange 21 . The loss of non-protein compound of protease enzymes seen with weight of 34 kDa, 17 kDa, 13 kDa.…”

Section: Discussionmentioning

confidence: 99%

Study of Uv Mutated Protease Enzyme From Various Sources

Saranya¹,

Dhanachezhiyan²,

Gopinath³

et al. 2019

Int Res J Pharm

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Proteases have wide variety of functions and commercial applications. Protease is the third largest groups of industrial enzymes and is used in detergents production, leather industry, food industry, pharmaceutical industry and bioremediation processes. Protease and amylase are well known industrially important enzymes. To study the UV mutated protease enzyme from various sources. Microbes were isolated from curd, buccal cavity are probiotics were maintained under optimum conditions, the microbial growth and enzyme production carried out at 37 º C for at 24 hours and pH 7.0. The isolated microbes were mutated using UV radiation exposure which enhanced protease and amylase enzymes production. The protease enzyme was confirmed using protease and amylase assay. The isolated bacteria have the ability to produce the industrially valuable enzymes which have various industrial applications. The protease enzyme has wide applications in many industries and therefore the UV mutated enzyme will have more thermostability.

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“…Bacillus cereus TD5B [11][12][13], Bacillus cereus LS2B [14][15][16] and Pseudomonas sp. PK-4 [17] was maintenance at the Laboratory of Leather Technology, By-products, and Livestock Waste, Gadjah Mada University.…”

Section: Indigenous Strains and Medium Preparationmentioning

confidence: 99%

“…PK-4 [17] was maintenance at the Laboratory of Leather Technology, By-products, and Livestock Waste, Gadjah Mada University. The strains originate from the soil at the chicken farm and Local Slaughterhouse [14,15]. One ose of the strains was input into the Pre-culture medium and incubated on a Rotary shaker at 120 rpm for 18 hours.…”

Section: Indigenous Strains and Medium Preparationmentioning

confidence: 99%

Effect of various poultry feather hydrolysates on the growth of indigenous keratinolytic strains

Fitriyanto

Ramadhanti

Rismiyati

et al. 2022

IOP Conf. Ser.: Earth Environ. Sci.

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Feather waste is a poultry by-product that is abundant, difficult to degrade, and creates an environmental problem. Feather protein is mainly composed of keratin, a structural protein with low digestibility. The effect of poultry feather meal prepared by NaOH as a Nitrogen source on the growth of the indigenous keratinolytic strain in the agar and the liquid medium was evaluated in this research. This study shows that all strains (Pseudomonas sp. PK-4, Bacillus cereus TD5B, and Bacillus cereus LS2B) can grow and produce clear zones around the colony. Medium containing 1% skim milk, commercial keratin, kampung, layer chicken feathers, and goose feathers were used to indicate that all strains could produce extracellular casein and keratinase enzymes. The strains can grow optimally in a liquid medium with feather hydrolysates, indicated by the increased turbidity (OD600) with a higher absorbance value. The highest growth occurred when strains grew with kampung chicken feather hydrolysate. Therefore, it can be concluded that the feather meals from local poultry feathers had potential as N-source for bacterial growth.

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Semi Purification and Identifications Molecule Protein Weigh of Alkaline Protease Enzyme from Bacillus cereus LS2B

Abstract: Abstract

Cited by 11 publications

References 16 publications

Enhanced catalytic activity of Bacillus aryabhattai P1 protease by modulation with nanoactivator

Enhanced catalytic activity of Bacillus aryabhattai P1 protease by modulation with nanoactivator

Study of Uv Mutated Protease Enzyme From Various Sources

Effect of various poultry feather hydrolysates on the growth of indigenous keratinolytic strains

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