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- Zhao, Hua; Tang, Jiayong; Cao, Lei; Jia, Gang; Long, Dingbiao; Liu, Guangmang; Chen, Xiaoling; Cai, Jingyi; Shang, Haiying
- Enzyme and microbial technology 2015 v.77 pp. 61-67
- Bacillus subtilis; Escherichia coli; Micrococcus luteus; Pichia pastoris; Staphylococcus aureus; agarose; amino acids; antibiotics; antimicrobial peptides; antimicrobial properties; complementary DNA; enteropeptidase; feed additives; feeds; genes; humans; lysozyme; molecular weight; nickel; synergism; yeasts
- ... Parasin I (PI) is a 19 amino acid peptide with potent antimicrobial activities against a broad spectrum of microorganisms and is a good candidate for development as a novel antimicrobial agent. The objective of this study was to express and characterize a codon optimized parasin I peptide fused with human lysozyme (hLY). A 513bp cDNA fragment encoding the mature hLY protein and parasin I peptide w ...
- Luo, Xi; Wang, Ya-Jun; Zheng, Yu-Guo
- Enzyme and microbial technology 2015 v.77 pp. 68-77
- Escherichia coli; Kluyveromyces marxianus var. lactis; NAD (coenzyme); alcohols; aldehydes; enzyme kinetics; genes; ketones; molecular weight; pH; substrate specificity
- ... An aldo-keto reductase gene (klakr) from Kluyveromyces lactis XP1461 was cloned and heterologously expressed in Escherichia coli. The aldo-keto reductase KlAKR was purified and found to be NADH-dependent with a molecular weight of approximately 36kDa. It is active and stable at 30°C and pH 7.0. The maximal reaction rate (vmax), apparent Michaelis–Menten constant (Km) for NADH and t-butyl 6-cyano-( ...