Analysis of Metabolic Functionality and Thermodynamic Feasibility of a Metagenomic Sample from “El Coquito” Hot Spring

2014 ◽  
pp. 287-293
Author(s):  
Maria A. Zamora ◽  
Andres Pinzón ◽  
Maria M. Zambrano ◽  
Silvia Restrepo ◽  
Linda J. Broadbelt ◽  
...  
Keyword(s):  
Hot Spring ◽  
Metagenomic Sample ◽  
Thermodynamic Feasibility

scholarly journals Comparative Analysis and Biochemical Characterization of Two Endo-β-1,3-Glucanases from the Thermophilic Bacterium Fervidobacterium sp.

Catalysts ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 830 ◽  
Author(s):  
Burkhardt ◽  
Schäfers ◽  
Claren ◽  
Schirrmacher ◽  
Antranikian
Keyword(s):  
Elevated Temperatures ◽  
Biochemical Characterization ◽  
Hot Spring ◽  
Biomass Conversion ◽  
Catalytic Efficiency ◽  
Industrial Applications ◽  
Thermophilic Bacterium ◽  
Metagenomic Sample ◽  
Wide Range ◽  
Active Site Cleft

Laminarinases exhibit potential in a wide range of industrial applications including the production of biofuels and pharmaceuticals. In this study, we present the genetic and biochemical characteristics of FLamA and FLamB, two laminarinases derived from a metagenomic sample from a hot spring in the Azores. Sequence comparison revealed that both genes had high similarities to genes from Fervidobacterium nodosum Rt17-B1. The two proteins showed sequence similarities of 62% to each other and belong to the glycoside hydrolase (GH) family 16. For biochemical characterization, both laminarinases were heterologously produced in Escherichia coli and purified to homogeneity. FLamA and FLamB exhibited similar properties and both showed highest activity towards laminarin at 90 °C and pH 6.5. The two enzymes were thermostable but differed in their half-life at 80 °C with 5 h and 1 h for FLamA and FLamB, respectively. In contrast to other laminarinases, both enzymes prefer β-1,3-glucans and mixed-linked glucans as substrates. However, FLamA and FLamB differ in their catalytic efficiency towards laminarin. Structure predictions were made and showed minor differences particularly in a kink adjacent to the active site cleft. The high specific activities and resistance to elevated temperatures and various additives make both enzymes suitable candidates for application in biomass conversion.

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

EFFECT OF BEACH NOURISHMENT ON HOT SPRING GROUNDWATER ENVIRONMENT IN IBUSUKI PORT COAST

2020 ◽  
Vol 76 (2) ◽  
pp. I_85-I_90
Author(s):  
Kenki KASAMO ◽  
Takatomo MIYAKE ◽  
Nobuyuki ONO ◽  
Kei GENPEI ◽  
Kotone Ota ◽  
...  
Keyword(s):  
Hot Spring ◽  
Beach Nourishment ◽  
Groundwater Environment
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