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( Xianghua Tang ),( Tianbao Luo ),( Xue Li ),( Huanhuan Yang ),( Yunjuan Yang ),( Junjun Li ),( Bo Xu ),( Zunxi Huang ) 한국미생물생명공학회(구 한국산업미생물학회) 2018 Journal of microbiology and biotechnology Vol.28 No.11
Enhanced application of solid-state fermentation (SSF) in industrial production and the influence of SSF of Rhizopus K1 on glucoamylase productivity were analyzed using the flat band method. A growth model was implemented through SSF of Rhizopus K1 in this experiment, and spectrophotometric method was used to determine glucoamylase activity. Results showed that in bran and potato culture medium with 70% moisture in a loose state, μ of mycelium reached to 0.15 h<sup>-1</sup> after 45 h of culture in a thermostatic water bath incubator at 30°C. Under a low-magnification microscope, mycelial cells appeared uniform, bulky with numerous branches, and were not easily ruptured. The generated glucoamylase activity reached to 55 U/g (dry basis). This study has good utilization value for glucoamylase production by Rhizopus in SSF.
( Tingting Yu ),( Junmei Ding ),( Qingxia Zheng ),( Nanyu Han ),( Jialin Yu ),( Yunjuan Yang ),( Junjun Li ),( Yuelin Mu ),( Qian Wu ),( Zunxi Huang ) 한국미생물 · 생명공학회 2016 Journal of microbiology and biotechnology Vol.26 No.4
est19 is a gene from Bacillus sp. K91 that encodes a new esterase. A comparison of the amino acid sequence showed that Est19 has typical Ser-Gly-Asn-His (SGNH) family motifs and could be grouped into the SGNH hydrolase family. The Est19 protein was functionally cloned, and expressed and purified from Escherichia coli BL21(DE3). The enzyme activity was optimal at 60°C and pH 9.0, and displayed esterase activity towards esters with short-chain acyl esters (C2-C6). A structural model of Est19 was constructed using phospholipase A1 from Streptomyces albidoflavus NA297 as a template. The structure showed an α/β-hydrolase fold and indicated the presence of the typical catalytic triad Ser49-Asp227-His230, which were further investigated by site-directed mutagenesis. To the best of our knowledge, Est19 is a new member of the SGNH hydrolase family identified from thermophiles, which may be applicable in the industrial production of semisynthetic β-lactam antibiotics after modification.