Molecular and biochemical characterization of an aminoalcoholphosphotransferase (AAPT1) from Brassica napus : effects of low temperature and abscisic acid treatments on AAPT expression in Arabidopsis plants and effects of over-expression of BnAAPT1 in transgenic Arabidopsis

Planta ◽  
2003 ◽  
Vol 217 (4) ◽  
pp. 547-558 ◽  
Author(s):  
Adrian J. Cutler ◽  
Suzanne R. Abrams ◽  
David C. Taylor ◽  
Qungang Qi ◽  
Yong-fen Huang
Keyword(s):  
Abscisic Acid ◽  
Brassica Napus ◽  
Low Temperature ◽  
Biochemical Characterization ◽  
Transgenic Arabidopsis ◽  
Over Expression ◽  
Acid Treatments

Cloning, Expression and Biochemical Characterization of the Recombinant α-amylase from Bacillus subtilis YX48

2021 ◽  
Vol 18 ◽  
Author(s):  
Yan Shan ◽  
Junjie Shang ◽  
Dongfang Zhang ◽  
Yinshan Cui ◽  
Yi Wang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Low Temperature ◽  
Biochemical Characterization ◽  
Amylase Activity ◽  
Heat Sensitivity ◽  
Medium Temperature ◽  
Temperature Environment ◽  
Structural Differences ◽  
Reduced Activity

Background: Amylase used in the market is mostly medium-temperature enzyme or high-temperature enzyme and has poor enzyme activity under low-temperature environment. Acid α-amylase can be used to develop digestion additives in the pharmaceutical and healthcare industries. The amino acid sequence and structural differences among α-amylases obtained from various organisms are high enough to confer interesting biochemical diversity to the enzymes. However, low- temperature (0-50℃) amylase, with an optimum temperature and heat sensitivity, has a greater potential value than medium (50-80℃) and high (80-110℃) temperature amylases. Methodology: The gene amy48 from encoding extracellular α-amylase in Bacillus subtilis YX48 was successfully cloned into the pET30a (+) vector and expressed in Escherichia coli BL21 (DE3) for biochemical characterization. Results and Conclusion: The molecular weight of α-amylase was 75 kDa. The activity of α-amylase was not affected by Ca2+, and Amy48 had the best activity at pH 5.0 and 37℃. AMY48 has high stability over a narrow pH and temperature range (5.0-8.0 and 30-45℃). Amylase activity was strongly inhibited by Zn2+, Mn2+, Cu2+, and Fe2+ ions, but Na+, K+, and Co2+ ions stimulate its activity slightly. The purified enzyme showed gradually reduced activity in the presence of detergents. However, it was remarkably stable against EDTA and urea.

Morphological, transcriptomics and biochemical characterization of new dwarf mutant of Brassica napus

Plant Science ◽  
2018 ◽  
Vol 270 ◽  
pp. 97-113 ◽  
Author(s):  
Chao Wei ◽  
Lixia Zhu ◽  
Jing Wen ◽  
Bin Yi ◽  
Chaozhi Ma ◽  
...  
Keyword(s):  
Brassica Napus ◽  
Biochemical Characterization ◽  
Dwarf Mutant
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