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        Intergeneric Hybridization between Streptomyces albulus and Bacillus subtilis Facilitates Production of ε-Poly-L-lysine from Corn Starch Residues

        Shu Li,Nan Wang,Zongjun Du,Guanjun Chen 한국생물공학회 2018 Biotechnology and Bioprocess Engineering Vol.23 No.5

        Intergeneric hybridization between S.albulus and B. subtilis to produce ε-poly-L-lysine (ε-PL) from corn starch residues (CSR) was investigated in this study. One hybrid, designated S. albulus LS-84, which incorporated the protease gene from B. subtilis, could effectively utilize the protein in CSR as a nitrogen source. In fed-batch fermentation, LS-84 produced 32.6 g/L ε-PL in the presence of 20 g/L CSR. This was an increase of 256.1% compared to that of the parent strain S. albulus LS-01. The rapid hydrolysis of CSR by protease caused rapid growth for LS- 84, which allowed higher respiratory activity. As a result, activities of several key enzymes in LS-84 were higher than those in LS-01; additionally, the content of several intracellular amino acids, such as Asp, Glu, and Arg, was also much higher in LS-84. Therefore, intergeneric hybridization between S. albulus and B. subtilis to produce ε-PL from CSR is an economical method for effective utilization of waste resources.

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        Isolation and Characterization of an Eosinophilic GH 16 β-Agarase (AgaDL6) from an Agar-Degrading Marine Bacterium Flammeovirga sp. HQM9

        ( Yan Liu ),( Xiaoxu Tian ),( Chao Peng ),( Zongjun Du ) 한국미생물 · 생명공학회 2019 Journal of microbiology and biotechnology Vol.29 No.2

        A special eosinophilic agarase exo-type β-agarase gene, AgaDL6, was cloned from a marine agar-degrading bacterium, Flammeovirga sp. HQM9. The gene comprised 1,383-bp nucleotides encoding a putative agarase AgaDL6 of 461 amino acids with a calculated molecular mass of 52.8 kDa. Sequence analysis revealed a β-agarase domain that belongs to the glycoside hydrolase family (GH) 16 and a carbohydrate-binding module (CBM_4_9) unique to agarases. AgaDL6 was heterologously expressed in Escherichia coli BL21 (DE3). Enzyme activity analysis of the purified protein showed that the optimal temperature and pH of AgaDL6 were 50°C and 3.0, respectively. AgaDL6 showed thermal stability by retaining more than 98% of activity after incubation for 2 h at 50°C, a feature quite different from other agarases. AgaDL6 also exhibited outstanding acid stability, retaining 100% of activity after incubation for 24 h at pH 2.0 to 5.0, a property distinct from other agarases. This is the first agarase characterized to have such high acid stability. In addition, we observed no obvious stimulation or inhibition of AgaDL6 in the presence of various metal ions and denaturants. AgaDL6 is an exo-type β-1,4 agarase that cleaved agarose into neoagarotetraose and neoagarohexaose as the final products. These characteristics make AgaDL6 a potentially valuable enzyme in the cosmetic, food, and pharmaceutical industries.

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