Biochemical characterization of a raw starch degrading α-amylase from the Indonesian marine bacterium Bacillus sp. ALSHL3

Biologia ◽  
2009 ◽  
Vol 64 (6) ◽  
Author(s):  
Keni Vidilaseris ◽  
Karina Hidayat ◽  
Debbie Retnoningrum ◽  
Zeily Nurachman ◽  
Achmad Noer ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Biochemical Characterization ◽  
Scanning Electron Micrographs ◽  
Bacillus Sp ◽  
Starch Granules ◽  
Raw Starch ◽  
Optimum Ph ◽  
Bacterium Bacillus ◽  
Rdna Analysis

AbstractAn Indonesian marine bacterial isolate, which belongs to genus of Bacillus sp. based on 16S rDNA analysis and was identified as Bacillus filicolonicus according to its morphology and physiology, produced a raw starch degrading α-amylase. The partially purified α-amylase using a maize starch affinity method exhibited an optimum pH and temperature of 6.0 and 60°C, respectively. The enzyme retained 72% of its activity in the presence of 1.5 M NaCl. Scanning electron micrographs showed that the α-amylase was capable of degrading starch granules of rice and maize. This α-amylase from Bacillus sp. ALSHL3 was classified as a saccharifying enzyme since its major final degradation product was glucose, maltose, and maltotriose.

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 Cloning and Characterization of a Cold-adapted Chitosanase from Marine Bacterium Bacillus sp. BY01

Molecules ◽  
2019 ◽  
Vol 24 (21) ◽  
pp. 3915 ◽  
Author(s):  
Yue Yang ◽  
Zhou Zheng ◽  
Yifei Xiao ◽  
Jiaojiao Zhang ◽  
Yu Zhou ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Marine Bacterium ◽  
Volume Concentration ◽  
Biological Activities ◽  
Maximum Activity ◽  
Bacillus Sp ◽  
Cold Adapted ◽  
Encoding Gene ◽  
Bacterium Bacillus

Chitosanase plays an important role in the production of chitooligosaccharides (CHOS), which possess various biological activities. Herein, a glycoside hydrolase (GH) family 46 chitosanase-encoding gene, csnB, was cloned from marine bacterium Bacillus sp. BY01 and heterologously expressed in Escherichia coli. The recombinant chitosanase, CsnB, was optimally active at 35 °C and pH 5.0. It was also revealed to be a cold-adapted enzyme, maintaining 39.5% and 40.4% of its maximum activity at 0 and 10 °C, respectively. Meanwhile, CsnB showed wide pH-stability within the range of pH 3.0 to 7.0. Then, an improved reaction condition was built to enhance its thermostability with a final glycerol volume concentration of 20%. Moreover, CsnB was determined to be an endo-type chitosanase, yielding chitosan disaccharides and trisaccharides as the main products. Overall, CsnB provides a new choice for enzymatic CHOS production.

Identification and Characterization of a New Alkaline SGNH Hydrolase from a Thermophilic Bacterium Bacillus sp. K91

2016 ◽  
Vol 26 (4) ◽  
pp. 730-738 ◽  
Author(s):  
Tingting Yu ◽  
Junmei Ding ◽  
Qingxia Zheng ◽  
Nanyu Han ◽  
Jialin Yu ◽  
...  
Keyword(s):  
Thermophilic Bacterium ◽  
Bacillus Sp ◽  
Bacterium Bacillus ◽  
Identification And Characterization

Biochemical Characterization of Raw-starch-digesting Alpha Amylase Purified from Bacillus amyloliquefaciens

2008 ◽  
Vol 158 (3) ◽  
pp. 653-662 ◽  
Author(s):  
Dhanya Gangadharan ◽  
K. Madhavan Nampoothiri ◽  
Swetha Sivaramakrishnan ◽  
Ashok Pandey
Keyword(s):  
Bacillus Amyloliquefaciens ◽  
Biochemical Characterization ◽  
Alpha Amylase ◽  
Raw Starch

Cloning, purification and biochemical characterization of beta agarase from the marine bacterium Pseudoalteromonas sp. AG4

2010 ◽  
Vol 37 (5) ◽  
pp. 483-494 ◽  
Author(s):  
Chulhong Oh ◽  
Chamilani Nikapitiya ◽  
Youngdeuk Lee ◽  
Ilson Whang ◽  
Se-Jae Kim ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Biochemical Characterization

scholarly journals Production and Characterization of Collagenase From Bacillus sp. 6-2 Isolated From Fish Liquid Waste

2019 ◽  
Vol 12 (1) ◽  
pp. 58
Author(s):  
Sartika Danial ◽  
Hasnah Natsir ◽  
Seniwati Dali ◽  
Leliani Leliani
Keyword(s):  
Liquid Waste ◽  
Industrial Applications ◽  
Selective Medium ◽  
Bacillus Sp ◽  
Fermentation Time ◽  
Collagen Peptides ◽  
Hydrolysis Products ◽  
Native Collagen ◽  
Optimum Ph

Collagenases are enzyme that are able to hydrolyze native collagen into fragment collagen peptides. Collagenases and its hydrolysis products have received tremendous attention in medical and industrial applications. The present study was conducted to isolate and identify new collagenase producing bacteria from fish liquid waste, then produce and characterize collagenase. A total of 7 isolate from fish liquid waste were screened on selective medium containg 2 % collagen and its activity was confirmed by the formation of clear zone. Isolat 6-2 was positif as collagenase producer and identified as Bacillus sp. 6-2 by morphological and biochemical characteristics. The optimum fermentation time of enzyme was investigated. Collagenase crude extract was characterized by the effect of pH, temperature, and metal ions. Isolat 62 optimally produced collagenase enzyme after 30 h of incubation with activity of   0.072 U/mL and protein content of 3.768 mg/mL. The optimum pH and temperature were 7.0 and 40 oC, respectively. The enzyme was activated by 1 mM Ca2+and  Mg2+, and inhibited by   1 mM  Zn2+ and Co2+. Collagenase from Bacillus sp. 6-2 may have potentials for medical and industrial applications.

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