다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기
Process biochemistry, v.45 no.4, 2010년, pp.451 - 456
Puri, Munish (Fermentation and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala 147002, India) , Kaur, Aneet (Fermentation and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala 147002, India) , Singh, R.S. (Fermentation and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala 147002, India) , Schwarz, Wolfgang H. (Department of Microbiology, Technische Universitaet Muenchen, Am Hochanger 4, D-85350 Freising-Weihenstephan, Germany) , Kaur, Amrit (Fermentation and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala 147002, India)
AI-Helper
Abstractα-L-Rhamnosidase (EC 3.2.1.40) is an enzyme that catalyzes the cleavage of terminal rhamnoside groups from naringin to prunin and rhamnose. In this study, a His-tag was genetically attached to the rhamnosidase gene ramA from Clostridium stercorarium to facilitate its purification from ...
J Mol Biol Cui 374 384 2007 10.1016/j.jmb.2007.09.003 Crystal structure of glycoside hydrolase family 78 α-l-rhamnosidase from Bacillus sp GL1
Enz Microb Technol Puri 18 281 1996 10.1016/0141-0229(95)00100-X Comparative kinetic characteristics of soluble and alginate entrapped naringinase
Appl Environ Microbiol Manzanares 67 2230 2001 10.1128/AEM.67.5.2230-2234.2001 Purification and characterization of two different α-l-rhamnosidases RhaA and RhaB from A. aculeatus
Biosci Biotechnol Biochem Yanai 64 2179 2000 10.1271/bbb.64.2179 Purification and characterization of intracellular alpha-l-rhamnosidase from Pichia angusta X349
Arch Biochem Biophys Hashimoto 415 235 2003 10.1016/S0003-9861(03)00231-5 Molecular identification of an α-l-rhamnosidase from Bacillus sp Strain GL1 as an enzyme involved in complete metabolism of gellan
Biotechnol Adv Puri 18 207 2000 10.1016/S0734-9750(00)00034-3 Production purification and characterization of the dibittering enzyme naringinase
J Antibiot Thirkettle 53 733 2000 10.7164/antibiotics.53.733 SB-253514 and analogues novel inhibitors of lipoprotein associated phospholipase A2 produced by Pseudomonas fluorescens M11579. III. Biotransformation using naringinase
Food Chem Busto 104 1177 2007 10.1016/j.foodchem.2007.01.033 Immobilization of naringinase from Aspergillus niger CECT 2088 in poly (vinyl alcohol) cryogels for the debittering of fruit juices
Curr Opin Struct Biol Davies 15 637 2005 10.1016/j.sbi.2005.10.008 Recent structural insights into the expanding world of carbohydrate-active enzymes
W J Microbiol Biotechnol Puri 21 753 2005 10.1007/s11274-004-5488-7 Purification and characterization of naringinase for the transformation of flavonoids
Puri 91 2008 Food enzymes: application of new technologies Immobilized enzymes for debittering citrus fruit juices
Mol Microbiol Zverlov 35 173 2000 10.1046/j.1365-2958.2000.01691.x The thermostable α-l-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of bacterial alpha-l-rhamnoside hydrolase, a new type of inverting glycoside hydrolase
Enz Microb Technol Birgisson 40 1181 2007 10.1016/j.enzmictec.2006.08.026 Immobilization of a recombinant E. coli producing a thermostable α-l-rhamnosidase: creation of a bioreactor for the hydrolysis of naringin
Appl Microbiol Biotechnol Koseki 80 1007 2008 10.1007/s00253-008-1599-7 Characterization of an α-l-rhamnosidase from Aspergillus kawachii and its gene
J Biochem Biophys Meth Chaga 49 313 2001 10.1016/S0165-022X(01)00206-8 Twenty five years of immobilized metal affinity chromatography: past, present and future
Nature Porath 258 598 1975 10.1038/258598a0 Metal chelate affinity chromatography a new approach to protein fractionation
Anal Biochem Paborsky 234 60 1996 10.1006/abio.1996.0050 A nickel chelate microtiter plate assay for six histidine containing proteins
Biomol Eng Puri 23 281 2006 10.1016/j.bioeng.2006.09.002 Focusing in on structural genomics; the University of Queensland structural biology pipeline
Appl Microbiol Biotechnol Tamai 80 627 2008 10.1007/s00253-008-1592-1 High level expression of His-tagged clostridial collagenase in Clostridium perfringes
J Chromatogr A Ueda 988 1 2003 10.1016/S0021-9673(02)02057-5 Current and prospective applications of metal ion-protein binding
Biochem Eng J Chi 39 376 2008 10.1016/j.bej.2007.10.008 Characterization of Bacillus kaustophilus leucine aminopeptidase immobilized in Ca-alginate/κ-carrageenan beads
Sambrook 2003 Molecular cloning: a laboratory manual
Nature Laemmli 227 680 1970 10.1038/227680a0 Cleavage of structural proteins during the assembly of the head of bacteriophage T4
Anal Biochem Bradford 72 248 1976 10.1016/0003-2697(76)90527-3 A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding
Appl Biochem Biotechnol Tung 136 1 2007 10.1007/BF02685934 Biochemical properties of genetic recombinant xylanase II
J Virol Meth Wizemann 77 189 1998 10.1016/S0166-0934(98)00152-9 Purification of E. coli-expressed His-tagged hepatitis B core antigen by Ni2+-chelate affinity chromatography
Nucleic Acids Res Cantarel 37 D233 2009 10.1093/nar/gkn663 The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics
Curr Microbiol Miyata 51 105 2005 10.1007/s00284-005-4487-8 Cloning, sequence analysis, and expression of the gene encoding Sphingomonas paucimobilis FP 2001 α-l-rhamnosidase
Enzyme Microbiol Technol Morana 39 1205 2006 10.1016/j.enzmictec.2006.03.010 Immobilization and characterization of a thermostable β-xylosidase to generate a usable biocatalyst
Appl Biochem Biotechnol Hung 150 157 2008 10.1007/s12010-008-8244-x Immobilization of Escherichia coli novablue γ-glutamultranspeptidase in Ca-alginate-κ-carrageenan beads
J Mol Catal B: Enzym Riberio 51 10 2008 10.1016/j.molcatb.2007.09.023 Kinetic modeling of naringin hydrolysis using a bitter sweet alfa-rhamnopyranosidase immobilized in k-carrageenan
Biosci Biotechnol Biochem Yanai 64 2179 2000 10.1271/bbb.64.2179 Purification and characterization of an α-l-rhamnosidase from Pichia angusta X349
Plant Physiol Mutter 106 241 1994 10.1104/pp.106.1.241 Rhamnogalactouronan α-l-rhamnopyranohydrolase. A novel enzyme specific for the terminal nonreducing rhamnosyl unit in rhamnogalacturonan regions of pectin
Arch Microbiol Miake 173 65 2000 10.1007/s002030050009 Purification and characterization of intracellular alpha-l-rhamnosidase from Pseudomonas paucimobilis FP2001
Arch Biochem Biophys Hashimoto 339 17 1997 10.1006/abbi.1996.9851 Microbial system for polysaccahride depolymerization: enzymatic route for gellan depolymerization by Bacillus sp. GL1
J Ferment Technol Tsen 66 193 1988 10.1016/0385-6380(88)90047-7 Comparison of the kinetics and factors affecting the stabilities of chitin immobilized naringinase from two fungal sources
Biotechnol Tech Ellenrieder 12 63 1998 10.1023/A:1008859627134 Hydrolysis of supersaturated naringin solutions by free and immobilized naringinase
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
Copyright KISTI. All Rights Reserved.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.