Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis

Tang, Xueming; Lakay, Francisco; Shen, Wei; Shao, Wei; Fang, Huiying; Prior, Bernard A.; Wang, Zhengxiang; Zhuge, Jian

doi:10.1023/b:bile.0000045642.19299.3f

Cited by 29 publications

(18 citation statements)

References 9 publications

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“…The enzyme was completely inhibited by 1 mM DFP, a well-known inhibitor of serine protease 4,21 suggesting that this enzyme was a serine protease. Similar results of serine proteases completely inhibited by DFP were observed in serine protease produced by B. licheniformis 22 , B. pumilus 7,21 and B. intermedius 3-19 23 . the enzyme under denaturing condition was estimated to be 27 kDa, similar to the molecular masses of alkaline proteases, which were in the ranges of 15 to 30 kDa 11 .…”

Section: Inhibitors Of the Protease Inhibitors Of The Protease Inhibisupporting

confidence: 80%

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Yossan¹,

Reungsang²,

Yasuda³

2006

ScienceAsia

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An alkaline protease produced by Bacillus megaterium isolated from a fermented broth of Thai fish sauce was purified by hydrophobic interaction combined with gel filtration techniques. After final purification step, the enzyme was purified 148-fold with an increase in specific activity from 0.09 to 13.33 U/mg protein.The properties of the purified enzyme were then analyzed. The molecular weight of the enzyme under denaturing condition was estimated to be 27 kDa. The optimum pH and temperature for protease activity were 10 and 50 o C, respectively. This protease could retain the activity in the pH and temperature ranging from pH 7.5 to 9.5 and 30 to 45 o C, respectively, resulting in the relative activity of higher than 80%. The enzyme was completely inhibited by diisopropyl fluorophosphate (DFP) suggesting that it was a serine protease. Phenylmethylsulfonyl fluoride (PMSF), p-Chloromercuribenzoic acid (PCMB), ethylenediaminetetraacetic acid (EDTA), 1, 10-phenanthroline and Fe 3+ strongly inhibited the activity of this purified enzyme activity, decreasing relative activity to lower than 15%. Protease activity was enhanced by Mn 2+ , Ca 2+ and Mg 2+ . Cytochrome C, soybean protein isolate and casein were good substrates specific to the enzyme with the relative activity of more than 100%.

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Section: Inhibitors Of the Protease Inhibitors Of The Protease Inhibisupporting

confidence: 80%

Untitled

Yossan¹,

Reungsang²,

Yasuda³

2006

ScienceAsia

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“…The ability of strain AK-R to grow over a wide range of NaCl concentrations (up to 25%), with maximum cells growth at 2.5-5% NaCl, indicated the halo-tolerance nature of this organism (JAIN et al, 2012). Studies on the effect of salinity on growth of halotolerant bacteria have shown a change in the polar lipid composition of the cell membranes and an increased salt concentration creates change in the lipid resulting in decrease of growth rate causing reduced enzyme production (TANG, X. M. et al, 2004). Strain AK-R and its extracellular alkaline protease with salt tolerance signify their potential application in laundry industry (HADDAR et al, 2009b).…”

Section: Effect Of Salinitymentioning

confidence: 99%

“…These cations probably protect the enzyme against thermal denaturation and therefore maintain the active conformation of the enzyme at high temperature (CHU, 2007). In addition; the inhibitory effect of other ions on alkaline protease is mostly attributed to metal catalyzed oxidation of amino acid residues essential to the enzyme activity (TANG et al, 2004). …”

Section: Effect Of Various Metalsmentioning

confidence: 99%

Alkaline protease from a new halotolerant alkaliphilic Bacillus agaradhaerens strain ak-r isolated from egyptian soda lakes

Ibrahim

Al‐Salamah

Elbadawi³

et al. 2016

Biosci. J.

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Alkaline proteases are hydrolytic enzymes that cleave peptide bonds in proteins and peptides in alkaline conditions, which occupy a pivotal importance with respect to their industrial applications. This study aimed to isolate new alkaline protease producing alkaliphilic bacteria from Egyptian soda lakes and optimize the fermentation process to enhance the enzyme production. The extensive screening process of the samples collected from Egyptian soda lakes resulted in isolation of a potent alkaline protease producing alkaliphilic strain AK-R. The isolate was identified as Bacillus agaradhaerens strain AK-R based on 16S rRNA gene analysis (99%). Wheat bran and gelatin supported maximum alkaline protease production as carbon and nitrogen sources, respectively. Strain AK-R is halo-tolerant thermotolerant alkaliphilic bacterium in nature, as it can grow over a wide range of NaCl concentrations (up to 25%) and up to 55 °C, with maximal growth and enzyme production at 2.5-5%, and pH 11 at 35 °C. Among the tested cations, only Mg 2+ and Ca 2+ ions significantly enhanced the enzyme production by about 1.2, and 1.3 fold compared to control, respectively. Alkaline protease secretion was coherent with the growth pattern, reaching maximal yield after about 32 h (mid stationary phase). In conclusion a new halo-tolerant thermo-tolerant alkaliphilic alkaline protease producing Bacillus agaradhaerens strain AK-R was isolated from Egyptian soda lakes. Optimization of the nutritional and cultivation conditions resulted in increase of enzyme yield by 20 fold. Strain AK-R and its extracellular alkaline protease with salt, pH and temperature, tolerance signify their potential application in laundry and pharmaceuticals industries.

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“…For instance A. flavus, Aspergillus niger and Aspergillus fumigutus were reported to produce enzymes essential in tannery industry (Barthomeuf et al, 1994). Thanikaivelan et al (2004) reported the potential of Aspergillus tamarii in tannery biotechnology whereas Aspergillus terreus was reported to produce tannery enzyme for processing leather (Tang et al, 2004).…”

Section: Aspergillus In Industrial Applicationmentioning

confidence: 99%

The potential of Aspergillus species in transformation of agricultural products for sustainable production of textile and leather industries in Tanzania

Zekeya¹,

Mtambo²,

Ndaro³

et al. 2017

Afr. J. Biotechnol.

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Manufacturing industries contribute about 8% of the gross domestic products (GDP) whereas leather and textile industries supply 18% employments of manufacturing industries in Tanzania. Manufacturing industries merely depend on agriculture for raw materials and other inputs. However, processing of leather and textiles requires a lot of inputs, many of them supplied from agricultural produce and some are imported from developed nations. In vast developing countries, including Tanzania, manufacturing industries are constrained by limited production technology and the allied costs than raw materials. The conventional processing of leather and textiles requires immense technological investment that is associated with high production cost. In Tanzania, inputs such as soaking, bating and tanning agents for tannery industries are expensive and sometimes not readily available due to importation costs. On the other hand, management of waste effluents from leather and textile processing is the major impediment for development of these industries. However, natural processing of covering materials by using fungal biotechnology is of great concern in Tanzania to avert the prevailing constrains. The application of fungal based biotechnology would reduce production cost and health consequences resulting from chemicals, particularly, chromium. The effects of toxic chemicals from leather and textile industries would be mitigated by employing non-viable Aspergillus biomass in the industrial processes.

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Purification and characterisation of an alkaline protease used in tannery industry from Bacillus licheniformis

Cited by 29 publications

References 9 publications

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Alkaline protease from a new halotolerant alkaliphilic Bacillus agaradhaerens strain ak-r isolated from egyptian soda lakes

The potential of Aspergillus species in transformation of agricultural products for sustainable production of textile and leather industries in Tanzania

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