Purification and characterization of a thermostable λ-carrageenase from a hot spring bacterium, Bacillus sp.

2014 ◽  
Vol 36 (8) ◽  
pp. 1669-1674 ◽  
Author(s):  
Jiang Li ◽  
Qiushi Hu ◽  
Dewi Seswita-Zilda
Keyword(s):  
Hot Spring ◽  
Bacillus Sp ◽  
Purification And Characterization ◽  
Bacterium Bacillus

scholarly journals Purification and Characterization of a Novel Alginate Lyase from the Marine Bacterium Bacillus sp. Alg07

Marine Drugs ◽  
2018 ◽  
Vol 16 (3) ◽  
pp. 86 ◽  
Author(s):  
Peng Chen ◽  
Yueming Zhu ◽  
Yan Men ◽  
Yan Zeng ◽  
Yuanxia Sun
Keyword(s):  
Marine Bacterium ◽  
Alginate Lyase ◽  
Bacillus Sp ◽  
Purification And Characterization ◽  
Bacterium Bacillus

scholarly journals PRODUCTION AND CHARACTERIZATION OF CHITINASE ENZYMES FROM SULILI HOT SPRING IN SOUTH SULAWESI, Bacillus sp. HSA,3-1a

2010 ◽  
Vol 10 (2) ◽  
pp. 256-260 ◽  
Author(s):  
Hasnah Natsir ◽  
Abd. Rauf Patong ◽  
Maggy Thenawidjaja Suhartono ◽  
Ahyar Ahmad
Keyword(s):  
Hot Spring ◽  
Thermophilic Bacteria ◽  
Extracellular Enzyme ◽  
Colloidal Chitin ◽  
Bacillus Sp ◽  
Optimum Temperature ◽  
South Sulawesi ◽  
Sds Page ◽  
Physiological Analysis

Chitinase is an extracellular enzyme which is capable in hydrolyzing insoluble chitin to its oligomeric and monomeric components. The enzyme produced by thermophilic bacteria was screened and isolated from Sulili hot spring in Pinrang, South Sulawesi, Indonesia. The gram positive spore forming rod shape bacteria was identified as Bacillus sp. HSA,3-1a through morphological and physiological analysis. The production of chitinase enzyme was conducted at various concentration of colloidal chitin at a pH of 7.0 and a temperature of 55 °C. The bacteria optimally was produced the enzyme at a colloidal chitin concentration of 0.5% after 72 h of incubation. The optimum temperature, pH and substrate concentration of chitinase were 60 °C, 7.0 and 0.3%, respectively. The enzyme was stable at a pH of 7.0 and a temperature of 60 °C after 2 h of incubation. The chitinase activities was increased by addition of 1 mM Mg2+, Ca2+ and Mn2+ ions, whereas the activities were  decreased by 1 mM Co2+, Fe2+ and Zn2 ions. The molecular weight of the crude enzyme was determined using SDS-PAGE analysis. Five protein fractions were obtained from SDS-PAGE, with MWs of 79, 71, 48, 43 and 22 kDa.   Keywords: colloidal chitin, thermophilic bacteria, chitinase

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