Enhanced Alkaline Protease Production in Addition to α-Amylase via Constructing a Bacillus subtilis Strain

Author(s):  
Taha I. Zaghloul ◽  
Abir E. Abdel Wahab ◽  
Mostafa H. Mostafa
2021 ◽  
Vol 16 (7) ◽  
pp. 84-91
Author(s):  
Maslinda Alias ◽  
Hakim Che Harun Mohammad ◽  
Ashraf Razali Nurul ◽  
Jasnizat Saidin ◽  
Nazaitulshila Rasit ◽  
...  

This research aims to produce thermostable alkaline protease from Bacillus subtilis isolated from La Hot Spring, Terengganu, Malaysia. The study was also conducted to determine the optimum conditions for protease production and stability by considering several parameters including pH, temperature and salt concentration. All seven bacteria were screened on skim milk agar overnight at 37 °C. Three strains with the highest proteolytic activity were identified in protease specific medium. The thermostable alkaline protease had an optimum temperature of 60 °C which achieved 85.73, 82.90 and 83.05 U/mL of protease activity for the three strains respectively. Furthermore, the strains exhibited significant activity of more than 90% from their original activity. Meanwhile, the optimum pH for protease production was pH 9 with the protease activity of 76.76, 79.71 and 88.39 U/mL for TB4, TB6 and TB9 strains, respectively. Proteases were found stable at pH 9 where the loss did not exceed 30% of its original activity. Collectively, all of the data emphasised that proteases from B. subtilis were alkaline thermostable proteases in accordance with a recent report. The finding highlights the viability of the proteases for biotechnological and industrial applications.


2017 ◽  
Vol 147 (5) ◽  
pp. 1204-1213 ◽  
Author(s):  
Fouzia Hussain ◽  
Shagufta Kamal ◽  
Saima Rehman ◽  
Muhammad Azeem ◽  
Ismat Bibi ◽  
...  

2016 ◽  
Vol 4 (3) ◽  
pp. 397-401
Author(s):  
M.D. BalaKumaran ◽  
R. Santhi

In the present study, chicken feather powder was screened for its application as the substrate for the production of keratinolytic protease by Bacillus subtilis strain PS03. Bacillus subtilis produced a high level of keratinolytic protease using chicken feather powder as substrate. With feather powder as substrate, physical factors such as incubation time, pH and temperature were optimized for increased keratinolytic protease production by Bacillus subtilis. The enzyme production was enhanced when using maltose as carbon source and yeast extract as nitrogen sources. SDS-PAGE analysis indicated the molecular weight of 46 kDa of the partially purified keratinolytic protease. The keratinolytic protease enzyme was stable over a pH range of 6 – 9 and temperature range of 35 - 50°C with maximum activity at pH 9 and 40°C. Based on the results, the use of feather powder as substrate for keratinolytic protease production is cost effective and is easy to scale up. Considering the availability and cost, chicken feather powder is considered as an ideal substrate for keratinolytic protease production in an industrial point of view. Int J Appl Sci Biotechnol, Vol 4(3): 397-401


2009 ◽  
Vol 191 (9) ◽  
pp. 3050-3058 ◽  
Author(s):  
Sadanobu Abe ◽  
Ayako Yasumura ◽  
Teruo Tanaka

ABSTRACT Expression of the gene for the extracellular alkaline protease (aprE) of Bacillus subtilis is subject to regulation by many positive and negative regulators. We have found that aprE expression was increased by disruption of the glutamine synthetase gene glnA. The increase in aprE expression was attributed to a decreased in expression of scoC, which encodes a negative regulator of aprE expression. The glnA effect on scoC expression was abolished by further disruption of tnrA, indicating that aprE expression is under global regulation through TnrA. In the scoC background, however, aprE expression was decreased by glnA deletion, and it was shown that the decrease was due to a defect in positive regulation by DegU. Among the genes that affect aprE expression through DegU, the expression of degR, encoding a protein that stabilizes phosphorylated DegU, was inhibited by glnA deletion. It was further shown that the decrease in degR expression by glnA deletion was caused by inhibition of the expression of sigD, encoding the σD factor, which is required for degR expression. In accordance with these findings, the expression levels of aprE-lacZ in glnA scoC degR and scoC degR strains were identical. These results led us to conclude that glnA deletion brings about two effects on aprE expression, i.e., a positive effect through inhibition of scoC expression and a negative effect through inhibition of degR expression, with the former predominating over the latter.


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