scholarly journals Scale-up thermostable α-amylase production in lab-scale fermenter using rice husk as an elicitor by Bacillus licheniformis-AZ2 isolated from Qinarje Hot Spring (Ardebil Prov. of Iran)

2018 ◽  
Vol 120 (1) ◽  
pp. 11-21 ◽  
Author(s):  
Ali Deljou
Keyword(s):  
Rice Husk ◽  
Bacillus Licheniformis ◽  
Hot Spring ◽  
Scale Up ◽  
Amylase Production

scholarly journals Production of thermostable extracellular α-amylase by a moderate thermophilic Bacillus licheniformis isolated from Qinarje Hot Spring (Ardebil prov. of Iran)

2017 ◽  
Vol 118 (4) ◽  
Author(s):  
Ali Deljou ◽  
Iman Arezi
Keyword(s):  
Carbon Source ◽  
Nitrogen Source ◽  
Bacillus Licheniformis ◽  
Bacterial Growth ◽  
Enzyme Production ◽  
Hot Spring ◽  
Basal Medium ◽  
Thermophilic Bacterium ◽  
Inoculum Size ◽  
Amylase Production

Background and Purpose: Amylases are most important industrial enzymes that account for about 30% of the world’s food, feed, fermentation, textile, detergent and cellulosic industries. This study aimed at optimum production of thermostable α-amylase via moderate thermophilic bacterium (Bacillus licheniformis) which was recently isolated from Qinarje Hot spring.Material and Methods: Initially, ability of bacterium for amylase activity was determined by starch hydrolysis test using Gram’s iodine staining. Then bacterial growth pattern and amylase production curves in basal production medium were graphically determined at different time intervals. Finally, effect of different temperature, pH, carbon source, nitrogen source, minerals and inoculum size were studied on bacterial growth and amylase production using turbidimetric and DNS method, respectively.Results: Optimum enzyme production achieved after 84 hours of inoculation from cultures growing at 40 ˚C and pH 9.0 in a medium containing 0.03% (w/v) of CaCl2, compared to the basal medium, results showed that the best enzyme production happened with inoculum size of 4% (v/v). The addition of 1% (w/v) rice husk (as a Carbon source) enhanced enzyme productivity up to 160% and substitution of the peptone and yeast extract with 1% (w/v) of tryptone (as a Nitrogen source) increased the α-amylase production up to 160%.Conclusion: Our findings show that B. licheniformis-AZ2 strain has an ability to produce the thermostable α-amylase which is suitable in starch processing and food industries. To be commercialized, further investigation is required for enhancement of the enzyme production.Keywords: Bacillus licheniformis; Optimization; Basal medium; Agricultural by-products.

scholarly journals Isolation and Characterisation of Thermophilic Bacillus licheniformis SUNGC2 as Producer of α-Amylase from Malaysian Hot Spring

2020 ◽  
Vol 28 (S2) ◽  
Author(s):  
Marwan Jawad Msarah ◽  
Ayesha Firdose ◽  
Izyanti Ibrahim ◽  
Wan Syaidatul Aqma
Keyword(s):  
Bacillus Licheniformis ◽  
Specific Activity ◽  
Hot Spring ◽  
Ammonium Phosphate ◽  
Fold Increase ◽  
Relative Activity ◽  
Biochemical Properties ◽  
Culture Conditions ◽  
Thermophilic Microorganisms ◽  
Amylase Production

Screening of new source of novel and industrially useful enzymes is a key research pursuit in enzyme biotechnology. The study aims to report the characteristics of novel thermophilic microorganisms isolated from Sungai Klah (SK) Hot Spring, Perak, Malaysia, that can produce α-amylase. The morphological and biochemical properties were examined for SUNGC2 sample. The isolate was further screened for amylase, followed by 16S rRNA and analytical profile index (API) test. This isolate was further subjected to pH optimisation for α-amylase production. It was found that SUNGC2 was an α-amylase producer and was identified as Bacillus licheniformis SUNGC2 with NCBI accession numbers MH062901. The enzyme was found to exhibit an optimum temperature of 50°C and a pH of 7.0. The relative activity of the enzyme was obtained based on the improvement of the culture conditions. The highest amount of amylase production was 24.65 U/mL at pH 7.0, consecutively the growth was also highest at pH 7.0 with a 9.45-fold increase in specific activity by ammonium phosphate precipitation of 80% (w/v). The results showed that the bacteria isolated from the hot spring are a significant source of thermophilic enzymes that are highly promising in biotechnology.

XYLANASE, AN ENVIRONMENTALLY FRIENDLY BLEACHING AGENT FOR PULP AND PAPER: Characterization And Stabilization Study Of Bacillus licheniformis I-5 CRUDE Xylanase

2018 ◽  
Vol 7 (3) ◽  
Author(s):  
Budiasih Wahyuntari., dkk
Keyword(s):  
Thermal Stability ◽  
Bacillus Licheniformis ◽  
Hot Spring ◽  
Sodium Dodecyl ◽  
Luria Broth ◽  
Crude Enzyme ◽  
Half Time ◽  
Triton X100 ◽  
Sds Page ◽  
Xylanolytic Enzymes

Isolate I-5 was isolated from Ciseeng hot spring, West Java and was identified as Bacillus licheniformis I-5. The isolate produces extracellular xylanolytic enzymes on Oatspelt containing Luria broth agar medium. Optimal activity of the crude enzyme was  observed at 50ºC and pH 7. The effect of sodium dodecyl sulphate, b-mercaptoethanol and Triton-X100 were observed. Incubating the crude enzyme in 1.5% SDS and 1.5% b-mercaptoethanol at 50oC for 90 minutes then adding Triton-X100 at final concentration of 3.5% for 45 minutes only reduced 5.75% of the initial enzyme activity. SDS/PAGE and zymogram analysis showed that at least two xylanolytic enzymes presence in the crude enzyme. The molecular weight of the enzyme was estimated about 127 and 20kD. The enzyme hydrolysed xylan into xylobiose, xylotriose and other longer xylooligosaccharides. Thermal stability of the crude enzyme was observed at 50, 60, and 70oC and pH 7 and 8. The results showed that the half time of the crude enzyme incubated at 50, 60, and 70oC pH 7 was 2 hours 55 minutes; 2 hours 33 minutes and 1 hour 15 minutes respectively. The half time at 50, 60 and 70oC, pH 8 was 2 hours 48 minutes; 1 hour 22 minutes and 1 hour 9 minutes respectively.keywords: Xilanase, Bacillus licheniformis I-5, thermal stability

Isolation and production of thermostable α-amylase from thermophilic Anoxybacillus sp. KP1 from Diyadin hot spring in Ağri, Turkey

Biologia ◽  
2014 ◽  
Vol 69 (4) ◽  
Author(s):  
Fatma Matpan Bekler ◽  
Kemal Güven
Keyword(s):  
Enzyme Activity ◽  
Hot Spring ◽  
Inorganic Nitrogen ◽  
Sodium Dodecyl ◽  
Maximum Growth ◽  
Casamino Acid ◽  
Rrna Gene ◽  
Amylolytic Enzyme ◽  
Amylase Production ◽  
Physiological Tests

AbstractA novel amylolytic enzyme producing thermophilic bacterial strain KP1 from the Diyadin hot spring water in Ağri, Turkey, was isolated in the present study. Phylogenetic analysis based on the partial 16S rRNA gene, biochemical and physiological tests revealed that the strain KP1 belongs to the genus Anoxybacillus. The pH and temperature optima for the α-amylase production by Anoxybacillus sp. KP1 were 8.0 and 50°C, respectively, where the maximum growth was obtained at the 28th hour of incubation and the highest α-amylase activity was obtained at the 40th hour of incubation (8979.6 U/mL). The optimum pH and temperature for the enzyme activity were 8.0 and 60°C, respectively. The maximum α-amylase production was secreted in the presence of 2% (w/v) soluble starch (10837.7 U/mL). Among the various organic and inorganic nitrogen sources tested, while keeping the beef extract concentration constant, casamino acid (14310.6 U/mL), urea (14126 U/mL), and tryptone (13217.2 U/mL) at a concentration of 2% gave the maximum α-amylase production. The enzyme activity was enhanced in the presence of 1.5 mM Mn2+ (123%), whereas it was strongly inhibited 1.5 mM by Hg2+. Inhibition by 89% was obtained also with sodium dodecyl sulphate (1%). The enzyme was found to be relatively stable at a range of pH and temperature.

Thermostable 1-amylase production by Bacillus licheniformis cells immobilized on polyacrylates with cyclic carbonate groups in the side chain

1998 ◽  
Vol 153 (2) ◽  
pp. 157-162 ◽  
Author(s):  
E. Dobreva ◽  
V. Ivanova ◽  
M. Stefanova ◽  
A. Tonkova ◽  
L. Kabaivanova ◽  
...  
Keyword(s):  
Bacillus Licheniformis ◽  
Cyclic Carbonate ◽  
Side Chain ◽  
Amylase Production
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