scholarly journals Optimization conditions of alkaline protease production by Streptomyces sp.H1 isolated from red sea coastal region in submerged culture

2018 ◽  
Vol 7 (3) ◽  
pp. 48
Author(s):  
Hind A. A. Al-Zahrani
Keyword(s):  
Red Sea ◽  
Alkaline Protease ◽  
Submerged Culture ◽  
Industrial Applications ◽  
Inoculum Size ◽  
Protease Production ◽  
High Yield ◽  
Partial Purification ◽  
Maximum Production ◽  
Beet Molasses

A potent alkaline protease producing strain characterized and identified as Streptomyces sp. H1 was isolated from soil around red sea shore. The enzyme was produced extracellulary in submerged culture revealed maximum level during early stationary phase. Alkaline protease showed the highest activity at incubation time, pH and inoculum size of 3 days, 9 and 8% respectively. Among different carbon sources beet molasses gave a maximum production followed by starch, sucrose and fructose. High yield of protease production was noticed with casein followed by peptone, yeast extract and ammonium sulphate. Furthermore, it was optimized with 7g/l NaCl resulted in higher level of protease. Optimization of the process parameters resulted in about 3.4 fold increase in the alkaline protease. Partial purification of the crude enzyme was achieved by fractional precipitation using ammonium sulfate at 50% saturation. Due to the maximum production of protease in the presence of cheaper substrate as beet molasses, stability at alkaline pH 9 and temperature up to 70 oC besides salt tolerance make the strain and its enzyme useful in different industrial applications.  

Production and characterisation of thermostable alkaline protease from Bacillus subtilis isolated from LA hot spring, Terengganu

2021 ◽  
Vol 16 (7) ◽  
pp. 84-91
Author(s):  
Maslinda Alias ◽  
Hakim Che Harun Mohammad ◽  
Ashraf Razali Nurul ◽  
Jasnizat Saidin ◽  
Nazaitulshila Rasit ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Alkaline Protease ◽  
Protease Activity ◽  
Hot Spring ◽  
Skim Milk ◽  
Industrial Applications ◽  
Protease Production ◽  
Significant Activity ◽  
Original Activity ◽  
Optimum Ph

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.

scholarly journals OPTIMIZATION OF CELLULASE ENZYME PRODUCTION FROM Aspergillus oryzae FOR INDUSTRIAL APPLICATIONS

2017 ◽  
Vol 2 (2) ◽  
pp. 155 ◽  
Author(s):  
Hassan Sher ◽  
Muhammad Faheem ◽  
Abdul Ghani ◽  
Rashid Mehmood ◽  
Hamza Rehman ◽  
...  
Keyword(s):  
Enzyme Production ◽  
Time Course ◽  
Value Added ◽  
Cellulase Production ◽  
Industrial Applications ◽  
Inoculum Size ◽  
Cellulosic Biomass ◽  
High Yield ◽  
Carboxymethyl Cellulase ◽  
Cellulase Enzyme

Cellulases are the hydrolytic group of enzymes, responsible for release of sugars in the bioconversion of the cellulosic biomass into a variety of value added industrial products. Fungal isolated cellulases are well studied and playing a significant role in various industrial processes. Enzymatic depolymerisation of cellulosic material has been done by the various fungal isolated enzymes. In the present study, the cultivation conditions for cellulase production from Aspergillus species were optimized. Optimization of scarification conditions such as time course, inoculum size, carbon source and concentration, nitrogen source, various pH levels were performed for the production of extracellular carboxymethyl cellulase and endoglucanase enzyme. The result exhibited, 15 % inoculums size, corncobs 2 % concentration, Urea and medium pH 7 at 30oC supported high yield of carboxymethyl cellulase (38.80 U/ml/min) and exoglucanase enzyme (10.94 U/ml/min) through a submerged fermentation (SmF). In future biotechnological applications in cellulase enzyme production attain a vital role to obtain high degradable yield.

scholarly journals Characterization and Optimization of Alkaline Protease Production from Bacillus licheniformis HSW-16 Isolated from Sambhar Salt Lake

2015 ◽  
Vol 3 (2) ◽  
pp. 347-351
Author(s):  
Rajnish Prakash Singh ◽  
Prabhat Nath Jha
Keyword(s):  
Bacillus Licheniformis ◽  
Alkaline Protease ◽  
Salt Lake ◽  
Industrial Applications ◽  
Protease Production ◽  
Protease Gene ◽  
Potential Source ◽  
Alkaline Protease Gene ◽  
Bacterium Bacillus ◽  
Ph Range

Halophilic microorganisms are recognized as potential source of secondary metabolites including enzymes and drugs with wide agricultural and industrial applications. In the present study protease producing halotolerant bacterium Bacillus licheniformis HSW-16 was isolated from hypersaline Sambhar lake, Rajasthan India. Protease production was performed by using azocasein as substrate. Confirmation of protease production was also done by amplification of alkaline protease gene and sequencing. The various nutritional factors such as carbon and nitrogen source and other physiological parameters like pH, temperature, incubation time and agitation speed were optimized for optimum protease production. The enzyme was active in pH range 7-10, temperature 25 °C-40 °C and salt concentration of 1.5M. The characteristics demonstrated by this isolate showed that it could be used as a potential source of enzyme.Int J Appl Sci Biotechnol, Vol 3(2): 347-351 DOI: http://dx.doi.org/10.3126/ijasbt.v3i2.12757 

scholarly journals Production, purification, and characterization of alkaline protease from Aspergillus flavus and its compatibility with commercial detergents

BioResources ◽  
2020 ◽  
Vol 16 (1) ◽  
pp. 291-301
Author(s):  
Amtul W. Wajeeha ◽  
M. Javaid Asad ◽  
Raja Tahir Mahmood ◽  
Tayyaba Zainab ◽  
Sidrah Nazir ◽  
...  
Keyword(s):  
Ammonium Sulphate ◽  
Aspergillus Flavus ◽  
Wheat Bran ◽  
Alkaline Protease ◽  
Growth Period ◽  
Nitrogen Sources ◽  
Protease Production ◽  
Gel Chromatography ◽  
Salting Out ◽  
Maximum Production

Aspergillus flavus was used to produce alkaline protease. Solid state fermentation (SSF) strategy was adopted to explore the most favorable physical and nutritional conditions for enzyme production. Maximum production was achieved at pH 6.0 and a temperature of 30 °C after 84 h of growth period. For the optimization of the chemical parameters, different carbon and nitrogen sources were used including glucose, fructose, sucrose, ammonium sulphate, and urea. Maximum production was observed with 0.3% concentration of all the compounds. Ammonium sulphate salting out and gel chromatography was used to purify the enzyme. The enzyme was completely precipitated out at 80% saturation. The value of Vmax was 3.9 U/mL, while the value of Km was 1.9 mg/mL. The enzyme was tested for its compatibility with a few famous detergents available on the market. With the alkaline protease under study, the enzyme displayed a maximum retention of its activity i.e. 80.8% in the presence of commercial detergent Surf excel. The activity dropped down to 61.5% when the enzyme was allowed to work in the presence of another locally used detergent, i.e., Bonus. Protease production from A. flavus was carried out on rice bran and wheat bran and the wheat bran gave better results.

scholarly journals Optimum growth conditions of Lactobacillus brevis LIPI13-2-LAB131 in β-galactosidase enzyme production

2020 ◽  
Vol 21 (11) ◽  
Author(s):  
Aafiyah Wahyu Nur Indah ◽  
ROHMATUSSOLIHAT ROHMATUSSOLIHAT ◽  
WINIATI PUDJI RAHAYU ◽  
FITRI SETYONINGRUM ◽  
GUNAWAN PRIADI ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Enzyme Production ◽  
Enzyme Purification ◽  
Incubation Temperature ◽  
Lactobacillus Brevis ◽  
Growth Conditions ◽  
Industrial Applications ◽  
Inoculum Size ◽  
Partial Purification ◽  
Optimum Growth

Abstract. Indah AWN, Rohmatussolihat, Rahayu WP, Setyoningrum F, Priadi G, Afianti F. 2020. Optimum growth conditions of Lactobacillus brevis LIPI13-2-LAB131 in β-galactosidase enzyme production. Biodiversitas 21: 5403-5407. Deficiency of β-galactosidase enzyme causes lactose to become undigested in gastrointestinal system, therefore the system needs further addition of external β-galactosidase. The sources β-galactosidase enzyme varies from plants, animals, and microorganisms. In industrial applications, microorganisms have become a considered potential source of β-galactosidase. Lactobacillus brevis LIPI13-2-LAB131 had high β-galactosidase enzyme activity, which was 7.93 U/mL. The aim of this research was to optimize the growth condition of L. brevis LIPI13-2-LAB131 in order to produce maximum β-galactosidase enzyme activity. This research consisted of performing optimization processes using design expert 7.0 (DX7) program with response surface methodology (RSM) and partial purification of β-galactosidase enzyme. The results of this research showed that the optimum growth conditions of L. brevis LIPI13-2-LAB131 were in 1.48% lactose level, incubation temperature of 34.91 °C, incubation time of 48.48 hours, and 2.83% inoculum size with desirability value of 0.839. The result of enzyme purification showed that value of β-galactosidase enzyme activity increased up to 22.88 ± 0.29 U/mL with purification yield of 11.65%.

scholarly journals Promising Immobilization of Industrial-Class Phospholipase A1 to Attain High-Yield Phospholipids Hydrolysis and Repeated Use with Optimal Water Content in Water-in-Oil Microemulsion Phase

2021 ◽  
Vol 11 (4) ◽  
pp. 1456
Author(s):  
Yusuke Hayakawa ◽  
Ryoichi Nakayama ◽  
Norikazu Namiki ◽  
Masanao Imai
Keyword(s):  
Water Content ◽  
Reaction Rate ◽  
Enzyme Reaction ◽  
Initial Reaction Rate ◽  
Industrial Applications ◽  
Molar Ratio ◽  
High Yield ◽  
Initial Reaction ◽  
Phospholipase A1 ◽  
Repeated Use

In this study, we maximized the reactivity of phospholipids hydrolysis with immobilized industrial-class phospholipase A1 (PLA1) at the desired water content in the water-in-oil (W/O) microemulsion phase. The optimal hydrophobic-hydrophilic condition of the reaction media in a hydrophobic enzyme reaction is critical to realize the maximum yields of enzyme activity of phospholipase A1. It was attributed to enzymes disliking hydrophobic surroundings as a special molecular structure for reactivity. Immobilization of PLA1 was successfully achieved with the aid of a hydrophobic carrier (Accurel MP100) combination with the treatment using glutaraldehyde. The immobilized yield was over 90% based on simple adsorption. The hydrolysis reaction was kinetically investigated through the effect of glutaraldehyde treatment of carrier and water content in the W/O microemulsion phase. The initial reaction rate increased linearly with an increasing glutaraldehyde concentration and then leveled off over a 6% glutaraldehyde concentration. The initial reaction rate, which was predominantly driven by the water content in the organic phase, changed according to a typical bell-shaped curve with respect to the molar ratio of water to phospholipid. It behaved in a similar way with different glutaraldehyde concentrations. After 10 cycles of repeated use, the reactivity was well sustained at 40% of the initial reaction rate and the creation of the final product. Accumulated yield after 10 times repetition was sufficient for industrial applications. Immobilized PLA1 has demonstrated potential as a biocatalyst for the production of phospholipid biochemicals.

Metabolic flux analyses for serine alkaline protease production

2000 ◽  
Vol 27 (10) ◽  
pp. 793-805 ◽  
Author(s):  
Pınar Çalik ◽  
Güzide Çalik ◽  
Serpil Takaç ◽  
Tunçer H Özdamar
Keyword(s):  
Alkaline Protease ◽  
Metabolic Flux ◽  
Protease Production ◽  
Serine Alkaline Protease

scholarly journals Purification, characterization and application of novel alkaline protease from new Bacillus cereus UV-15 mutant

2017 ◽  
Vol 7 (4) ◽  
pp. 1 ◽  
Author(s):  
Sreedevi Basavaraju ◽  
Chandrasekhar Kathera ◽  
Pramoda Kumari Jasti
Keyword(s):  
Bacillus Cereus ◽  
Ammonium Sulphate ◽  
Alkaline Protease ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Industrial Applications ◽  
Tween 20 ◽  
Original Activity ◽  
Protease Enzyme

The alkaline protease produced by Bacillus cereus UV-15 mutant was purified by precipitation with ammonium sulphate and gel filtration through sephadex G-100. The enzyme has shown to have a molecular weight of 29kDa by SDS polyacrylamide gel electrophoresis. The extracted protease enzyme was purified by 16.64 fold through ammonium sulphate precipitation and chromatography separation in Sephadex G-100. The purified protease had a specific activity of 2915 (U/mg). The zymogram also revealed a clear hydrolytic zone due to proteolytic activity, which coincided with the band obtained with SDS–PAGE. The enzyme was remained active and stable at pH 8-11, with an optimum at pH 10.0. The protease was stable in the temperature ranging from 40°C to 60°C, but gradually decreased at temperature 70°C. The optimum temperature for protease activity was determined at 60°C. The enzyme showed stability towards non-ionic and anionic surfactants, and oxidizing agents. At 1% concentration of Tween-20 and Tween-80, the enzyme retained 78% and 94% relative activity respectively. Alkaline protease retained 95% activity toward 0.5% concentration of the anionic detergent SDS. The enzyme showed compatibility at 50°C with commercial detergents such as Ariel, Surf excel, Rin, wheel, Tide and Nirma. In the presence of Ariel and Rin the enzyme retained about 72 and 75% of the original activity respectively. The supplementation of the enzyme in detergents could improve the cleansing performance towards the blood stains and suggested to be used as a detergent additive. The enzyme also removed goat hide hairs completely after 15 hr of incubation. These characteristics may make the enzyme suitable for several industrial applications, especially in leather industries.

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