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tom 57
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nr 3
EN
 A lipase gene SR1 encoding an extracellular lipase was isolated from oil-contaminated soil and expressed in Escherichia coli. The gene contained a 1845-bp reading frame and encoded a 615-amino-acid lipase protein. The mature part of the lipase was expressed with an N-terminal histidine tag in E. coli BL21, purified and characterized biochemically. The results showed that the purified lipase combines the properties of Pseudomonas chlororaphis and other Serratia lipases characterized so far. Its optimum pH and temperature for hydrolysis activity was pH 5.5-8.0 and 37ºC respectively. The enzyme showed high preference for short chain substrates (556.3 ± 2.8 U/μg for C10 fatty acid oil) and surprisingly it also displayed high activity for long-chain fatty acid. The deduced lipase SR1 protein is probably from Serratia, and is organized as a prepro-protein and belongs to the GXSXG lipase family.
EN
Support vector machine and artificial neural network are widely used in classification applications. Extreme learning machine (ELM) is a novel and efficient learning algorithm based on the generalized single hidden layer feed forward networks, which performs well in classification applications. The research results have shown the superiority of ELM with the existing classical algorithms: support vector machine (SVM) and back propagation neural network. In this study, we firstly propose a novel nonnegative matrix factorization extreme learning machine (NMFELM) to improve the performance of standard ELM method. Then we propose a novel near-infrared palmprint recognition approach based on NMFELM classifier. As the test data, we use the near-infrared palmprint database provided by Hong Kong Polytechnic University. The experimental results demonstrate that the proposed NMFELM method outperforms the standard ELM- and SVM-based methods.
EN
A full-length cDNA of a new serine/threonine (Ser/Thr) protein kinase gene, designated as BnSOS2 (GenBank Acc. No.AY310413), was cloned from Brassica napus by rapid amplification of cDNA ends (RACE). The fulllength cDNA of BnSOS2 was 1779 bp and contained a 1539-bp open reading frame encoding a protein of 512 amino acids. Homology analysis shows that BnSOS2 strongly resembles other Ser/Thr protein kinase genes, and that its putative protein belongs to a typical Ser/Thr kinase family. Northern blot analysis reveals that BnSOS2 is salt-inducible. Our results indicate that BnSOS2 is a new member of the plant SOS2 gene family, which may play an important role in salt tolerance of plants.
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