A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

Benmrad, Maroua Omrane; Moujehed, Emna; Elhoul, Mouna Ben; Jaouadi, Nadia Zaraî; Mechri, Sondes; Rekik, Hatem; Kourdali, Sidali; Hattab, Mohamed El; Badis, Abdelmalek; Sayadi, Sami; Béjar, Samír; Jaouadi, Bassem

doi:10.1016/j.ijbiomac.2016.06.025

Cited by 42 publications

(21 citation statements)

References 55 publications

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“…With 5.0 mM Ca 2+ , the optimal temperature increased to 70 °C. The upward shift of optimal temperature by Ca 2+ has been reported for SPTC protease from Trametes cingulate 52 . In addition, adding Ca 2+ also broadened the temperature range where more than 60.0% of activity was maintained.…”

Section: Resultsmentioning

confidence: 56%

“…AprA exhibits higher optimal pH (10.5) and better stability under alkaline conditions than many previously reported alkaline proteases from Bacillus 4 , 6 , 8 , 9 , 15 , 16 , 27 , 33 , 51 , 56 – 61 , Vibrio 19 , Aspergillus 21 , 62 , 63 , Thermoactinomyces 24 , 26 , Streptomyces 25 , Thermus 28 , Pseudoalteromonas 41 , Alteromonas 42 , Stenotrophomonas 44 , Trametes 52 , Termitomyces 54 , Virgibacillus 64 , Caldicoprobacter 65 , Hirsutella 66 , Scopulariopsis 67 , and Penicillium 68 (Table S1 ). Furthermore, AprA also retains high activity and stability over a wide range of pH (7.0–11.5) and temperature (40–70 °C), several metal ions, surfactants and some oxidizing and reducing agents.…”

Section: Discussionmentioning

confidence: 81%

“…These ions have been reported to activate proteases from organisms such as Caldicoprobacter guelmensis 75 , Streptomyces koyangensis 25 , T. cingulate 52 , and Bacillus circulans 56 . These studies suggest that the bivalent ions may stabilize enzyme structure, especially the active conformation at high temperature and protect the enzyme against thermal denaturation 5 , 47 , 52 . However, Cu 2+ , Ba 2+ , and Co 2+ found to be inhibitory in these studies can stimulate AprA and AprA-PPC.…”

Section: Discussionmentioning

confidence: 99%

“…On the other hand, the activity of AprA and AprA-PPC was significantly but not completely inhibited by certain other bivalent ions including Hg 2+ , Pb 2+ , Ni 2+ , Fe 2+ , Zn 2+ , and the monatomic ion of Ag + . These toxic metallic ions might bind to particular organic ligands resulting in enzyme denaturation 52 . Notably, the inhibitory effect of heavy metallic ions such as Hg 2+ and Pb 2+ has been found to be a common phenomenon in many enzymes including proteases and is well documented in the literature.…”

Section: Discussionmentioning

confidence: 99%

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A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry

Zhou

Qin

Chen

et al. 2018

Sci Rep

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Alkaline proteases have a myriad of potential applications in many industrial processes such as detergent, food and feed production, waste management and the leather industry. In this study, we isolated several alkaline protease producing bacteria from soda lake soil samples. A novel serine alkaline protease (AprA) gene from alkaliphilic Idiomarina sp. C9-1 was cloned and expressed in Escherichia coli. The purified AprA and its pre-peptidase C-terminal (PPC) domain-truncated enzyme (AprA-PPC) showed maximum activity at pH 10.5 and 60 °C, and were active and stable in a wide range of pH and temperature. Ca2+ significantly improved the thermostability and increased the optimal temperature to 70 °C. Furthermore, both AprA and AprA-PPC showed good tolerance to surfactants and oxidizing and reducing agents. We found that the PPC domain contributed to AprA activity, thermostability and surfactant tolerance. With casein as substrate, AprA and AprA-PPC showed the highest specific activity of 42567.1 U mg−1 and 99511.9 U mg−1, the Km values of 3.76 mg ml−1 and 3.98 mg ml−1, and the Vmax values of 57538.5 U mg−1 and 108722.1 U mg−1, respectively. Secreted expression of AprA-PPC in Bacillus subtilis after 48 h cultivation resulted in yield of 4935.5 U ml−1 with productivity of 102.8 U ml−1 h−1, which is the highest reported in literature to date. Without adding any lime or sodium sulfide, both of which are harmful pollutants, AprA-PPC was effective in dehairing cattle hide and skins of goat, pig and rabbit in 8–12 h without causing significant damage to hairs and grain surface. Our results suggest that AprA-PPC may have great potentials for ecofriendly dehairing of animal skins in the leather industry.

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Section: Resultsmentioning

confidence: 56%

Section: Discussionmentioning

confidence: 81%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry

Zhou

Qin

Chen

et al. 2018

Sci Rep

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“…In contrast, it was reported that Mn 2+ , Ca 2+ and Mg 2+ ions have increased the relative protease activity of Bacillus megaterium isolated from Thai fish sauce 27 . Following the addition of MnCl 2 and CaCl 2 , the activity of alkaline protease from Trametes cingulata strain CTM10101 was enhanced by 170 and 219%, respectively 28 . This shows that there is no standard cofactor for enhancement of protease activity.…”

Section: Resultsmentioning

confidence: 99%

Production of thermotolerant, detergent stable alkaline protease using the gut waste of Sardinella longiceps as a substrate: Optimization and characterization

Ramkumar

Sivakumar

Gujarathi

et al. 2018

Sci Rep

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The gut wastes of Sardinella longiceps were used as substrate for protease production. The gut waste has 61.6% proteins, 21.8% lipids, 8.5% carbohydrates on dry weight basis and trace elements. The significant factors of protease fermentation were screened by Plackett-Burman design. A protease activity of 68.56 U/ml was predicted at 46.31 °C, incubation time 71.11 h, inoculum 4.86% (v/v) and substrate concentration 2.66% (w/v), using response surface methodology. However, the validation experiment showed 73.52 U/ml activity. The artificial neural network was found as a better tool to predict the experimental results. The partially purified protease showed higher activity at pH 9 and 10 and retained 90% activity after 120 h at pH 9. It showed maximum activity at 50 °C and retained 88% residual activity until 90 min at 50 °C. Zn++ enhanced the protease activity by 40%. The protease retained an activity of 93, 103, 90 and 98% against urea, β-mercaptoethanol, SDS and tween 80 respectively. The alkaline protease was compatible with all the commercial detergents tested with the residual activity above 90%. The alkaline protease exhibited 22% higher activity on the tryptone soya substrate. The gut waste of S. longiceps is a worthy low cost substrate for the production of industrially important alkaline protease.

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Microbial Alkaline Protease: Production, Purification, and Applications

Tadesse,

Ayele,

Korsa

et al. 2024

Microbial Enzymes

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A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

Cited by 42 publications

References 55 publications

A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry

A novel alkaline protease from alkaliphilic Idiomarina sp. C9-1 with potential application for eco-friendly enzymatic dehairing in the leather industry

Production of thermotolerant, detergent stable alkaline protease using the gut waste of Sardinella longiceps as a substrate: Optimization and characterization

Microbial Alkaline Protease: Production, Purification, and Applications

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