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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.
Zhang, Guobing,Li, Peng,Tang, Longxiang,Ma, Jingxuan,Wang, Xianghua,Lu, Hongbo,Kang, Boseok,Cho, Kilwon,Qiu, Longzhen The Royal Society of Chemistry 2014 Chemical communications Vol.50 No.24
<P>A bis(2-oxoindolin-3-ylidene)-benzodifuran-dione (BIBDF)-based low band gap polymer (PBIBDF-BT), containing a solubilizing alkyl chain bithiophene unit as a donor, has been synthesized. The polymer with a low-lying LUMO/HOMO energy level (−4.03/−5.55 eV) exhibits efficient ambipolar charge transport. The electron and hole mobilities are as high as 1.08 and 0.30 cm<SUP>2</SUP> V<SUP>−1</SUP> s<SUP>−1</SUP>, respectively.</P> <P>Graphic Abstract</P><P>The PBIBDF-BT polymer exhibits high ambipolar charge transport with electron and hole mobilities as high as 1.08 and 0.30 cm<SUP>2</SUP> V<SUP>−1</SUP> s<SUP>−1</SUP>, respectively. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c3cc48695h'> </P>
JunPei Zhou,Yanyan Dong,Yajie Gao,Xianghua Tang,Junjun Li,YUN-JUAN YANG,Bo Xu,Zhenrong Xie,Zunxi Huang 한국생물공학회 2012 Biotechnology and Bioprocess Engineering Vol.17 No.4
The 774-bp pectate lyase gene plyAI4 from Bacillus sp. I4 was cloned and expressed in E. coli. The gene encodes a 257-residue polypeptide (PlyAI4, 28.3 kDa)with the highest identities of 97.3% with a putative pectate lyase from Bacillus subtilis BSn5 (ADV94306) and 60.3%with an identified pectate lyase of the polysaccharide lyase family (PL) 3 from Paenibacillus amylolyticus 27C64(ADB78774). The purified recombinant PlyAI4 (rPlyAI4)exhibited apparently optimal activity at pH 10.5 ~ 11.0 and 50oC. Compared with the majority of reported alkaline pectate lyases, rPlyAI4 exhibited more residual enzyme activity at 20oC (~45%) or at 70oC (~50%) and better thermostability at 70oC (~60 min half-life at 70oC). In the presence of 20% (v/v) ethanol, pectate lyase activity was enhanced by 0.2 fold. After incubation in 40% (v/v)ethanol at 37oC and pH 8.5 for 1 h, the purified rPelAI4retained more than 75% of the initial activity. Sequence analysis proposed a new signature block, A-D-G-[V/I]-H,for PL 3 pectate lyases. These properties may prove to be important with regards to PlyAI4 for basic research and industrial application.
( Jun Pei Zhou ),( Yan Yan Dong ),( Jun Jun Li ),( Rui Zhang ),( Xianghua Tang ),( Yuelin Mu ),( Bo Xu ),( Qian Wu ),( Zun Xi Huang ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.11
The α-galactosidase-coding gene agaAJB13 was cloned from Sphingomonas sp. JB13 showing 16S rDNA (1,343 bp) identities of ≤97.2% with other identified Sphingomonas strains. agaAJB13 (2,217 bp; 64.9% GC content) encodes a 738-residue polypeptide (AgaAJB13) with a calculated mass of 82.3 kDa. AgaAJB13 showed the highest identity of 61.4% with the putative glycosyl hydrolase family 36 α-galactosidase from Granulicella mallensis MP5ACTX8 (EFI56085). AgaAJB13 also showed <37% identities with reported protease-resistant or Sphingomonas α-galactosidases. A sequence analysis revealed different catalytic motifs between reported Sphingomonas α-galactosidases (KXD and RXXXD) and AgaAJB13 (KWD and SDXXDXXXR). Recombinant AgaAJB13 (rAgaAJB13) was expressed in Escherichia coli BL21 (DE3). The purified rAgaAJB13 was characterized using p-nitrophenyl-α-D-galactopyranoside as the substrate and showed an apparent optimum at pH 5.0 and 60oC and strong resistance to trypsin and proteinase K digestion. Compared with reported proteaseresistant α-galactosidases showing thermolability at 50oC or 60oC and specific activities of <71 U/mg with or without protease treatments, rAgaAJB13 exhibited a better thermal stability (half-life of >60 min at 60oC) and higher specific activities (225.0-256.5 U/mg). These sequence and enzymatic properties suggest AgaAJB13 is the first identified and characterized Sphingomonas α-galactosidase, and shows novel protease resistance with a potential value for basic research and industrial applications.