耐高温α-淀粉酶-Alpha-amylase 产品参数 耐高温α-淀粉酶采用地衣芽孢杆菌(Bacillus licheniformis),经发酵、提取精制而成。本品具有特别好的耐高温特性。广泛应用于酒精、啤酒、制醋、酱油、纺织、印染、造纸及其他发酵领域。 The high-temperature resistant alpha-amylase is made from Bacillus licheniformis (Bac...
High temperature alpha-amylase gene is obtained from Thermoanaerobacter tengcongensis MB4 total DNA to constitute prokaryotic expression plasmid and transferred to colibacillus for expression. Amino acid sequence comparison shows that the alpha-amylase is one new kind of alpha-amylase....
The heat resistance of alpha-amylase has become a hot research topic.This paper expounds the research significance of high thermal stability of alpha-amylase;summarized the source of alpha-amylase and lists some main microbial source of high temperature of alpha-amylase.It reviewedfactors influencing...
The effects of excessive expression of degQ gene on the expression of high temperature α-amylase of Bacillus licheniformis(BL) were studied.degQ gene was obtained from BL genome through PCR amplification,and cloned it into pHY-P43 vector and got pHY-P43-degQ recombinant plasmid.It was then ...
产品名称:Human Salivary Lyophilized High Purity Alpha-Amylase (A-Amylase) 产品型号:IRHPL0049 产品展商:Innov-Research 产品文档:无相关文档 简单介绍 Human Salivary Lyophilized High Purity Alpha-Amylase (A-Amylase) Human Salivary Lyophilized High Purity Alpha-Amylase (A-Amylase)的详细介绍 ...
alpha-Amylase (Amylase, AMY), as the name implies, is an enzyme that hydrolyzes starch into glucose, maltose, oligosaccharides and dextrins. It is ma..
Declerck N, Machius M, Wiegand G, Huber R, Gaillardin C: Probing structural determinants specifying high thermostability in Bacillus licheniformis alpha-amylase. J Mol Biol 2000, 301(4):1041-1057.Declerck N,Machius M,Wiegand G,et al. Probing Structural Determinants Specifying High ...
Alpha-amylase activity of wheat grain from crops differing in grain drying rate The hypothesis was tested that slow grain drying stimulates pre-maturity alpha-amylase activity in wheat (Triticumaestivum L.). Grain drying rate in 91 com... PS Kettlewell,MM Cashman - 《Journal of Agricultural Sci...
licheniformis alpha-amylase structure. It is found on the C domain where it bridges the two beta-sheets. Three acid residues (Glu261, Asp328, and Asp231) form an active site similar to that seen in other amylases. In the presence of TRIS buffer, a single molecule of TRIS occupies the ...
Suppression of alpha-amylase genes improves quality of rice grain ripened under high temperature. Plant Biotechnol J. 2012;10(9):1110–7. Article CAS PubMed Google Scholar Larkin PD, Park WD. Transcript accumulation and utilization of alternate and non-consensus splice sites in rice granule-...