다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기
Bioscience, biotechnology, and biochemistry, v.78 no.9, 2014년, pp.1537 - 1541
Kataoka, Misumi (Biomass Refinery Research Center, National Institute of Advanced Industrial Science and Technology (AIST), Higashi-Hiroshima, Japan) , Ishikawa, Kazuhiko (Biomass Refinery Research Center, National Institute of Advanced Industrial Science and Technology (AIST), Higashi-Hiroshima, Japan)
AI-Helper
AbstractHyperthermophilic cellulase is an industrially important enzyme for biomass saccharification at high temperature. Two hyperthermophilic cellulases from the hyperthermophile Pyrococcus furiosus, endocellulase (EGPf) and β-glucosidase (BGLPf), exhibit optimal activity at 90-105 °C and...
Biosci. Biotechnol. Biochem Pang 69 553 2005 10.1271/bbb.69.553 Structure of β-glucan oligomer from laminarin and its effect on human monocytes to inhibit the proliferation of U937 cells
Extremophiles González 2 123 1998 10.1007/s007920050051 Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough
Nature Lipp 454 991 2008 10.1038/nature07174 Significant contribution of Archaea to extant biomass in marine subsurface sediments
FEBS Lett Kim 586 1009 2012 10.1016/j.febslet.2012.02.029 Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the DxDxDG calcium-binding motif in Pyrococcus furiosus
Proteins Kim 78 496 2010 10.1002/prot.22602 Structure of hyperthermophilic endocellulase from Pyrococcus horikoshii
J. Bacteriol Bauer 181 284 1999 10.1128/JB.181.1.284-290.1999 An endoglucanase, EglA, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes β-1,4 bonds in mixed-linkage (1→3),(1→4)-β-D-glucans and cellulose
Appl. Environ. Microbiol Ando 68 430 2002 10.1128/AEM.68.1.430-433.2002 Hyperthermostable endoglucanase from Pyrococcus horikoshii
Appl. Environ. Microbiol Wang 77 5199 2011 10.1128/AEM.00199-11 High-temperature enzymatic breakdown of cellulose
Eur. J. Biochem Kengen 213 305 1993 10.1111/ejb.1993.213.issue-1 Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
Acta Cryst Kado F67 1473 2011 Structure of hyperthermophilic β-glucosidase from Pyrococcus furiosus
Acta Cryst Nakabayashi D70 877 2014 Structural analysis of β-glucosidase mutants derived from a hyperthermophilic tetrameric structure
Extremophiles Kashima 9 37 2005 10.1007/s00792-004-0418-z Analysis of the function of a hyperthermophilic endoglucanase from Pyrococcus horikoshii that hydrolyzes crystalline cellulose
Acta Cryst Kataoka F68 328 2012 Crystallization and preliminary X-ray analysis of a hyperthermophilic endoglucanase from Pyrococcus furiosus
Anal. Biochem Gill 182 319 1989 10.1016/0003-2697(89)90602-7 Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem
Biochemistry Kaper 39 4963 2000 10.1021/bi992463r Comparative structural analysis and substrate specificity engineering of the hyperthermostable β-glucosidase CelB from Pyrococcus furiosus
Biochem. Z Michaelis 49 333 1913 Die Kinetik der Invertinwirkung
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
출판사/학술단체 등이 한시적으로 특별한 프로모션 또는 일정기간 경과 후 접근을 허용하여, 출판사/학술단체 등의 사이트에서 이용 가능한 논문
Copyright KISTI. All Rights Reserved.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.