Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04

Applied Microbiology and Biotechnology

Volumn 98, Issue 5, 2014, Pages 2121-2131

  Jung, Jong Hyun ^a   Seo, Dong Ho ^a   Holden, James F ^b   Park, Cheon Seok ^a  

^a Kyung Hee University   (South Korea)

^b UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

Hyperthermophile; Maltose inhibition; Maltose forming amylase; Pyrococcus sp. ST04

Indexed keywords

AMINO ACID SEQUENCE; GLUCANOTRANSFERASE; GLYCOSIDE HYDROLASES; HYDROLYTIC ACTIVITIES; HYPERTHERMOPHILES; HYPERTHERMOPHILIC ARCHAEON; MALTOOLIGOSACCHARIDES; PYROCOCCUS SP. ST04;

AMINO ACIDS; AMYLASES; CLONING; CYCLODEXTRINS; ESCHERICHIA COLI; GENES; HYDROLYSIS; MICROORGANISMS; MONOPOLE ANTENNAS;

MALTOSE;

6 O GLUCOSYL BETA CYCLODEXTRIN; AMYLASE; BETA CYCLODEXTRIN; CYCLODEXTRIN DERIVATIVE; MALTOSE; PULLULAN; UNCLASSIFIED DRUG;

BACTERIUM; ENZYME ACTIVITY; HYDROLYSIS; INHIBITION; RECOMBINATION; THERMOPHILY;

ARTICLE; BACTERIAL GENE; ESCHERICHIA COLI; GENE EXPRESSION; MOLECULAR CLONING; NONHUMAN; PYROCOCCUS;

ARCHAEA; ESCHERICHIA COLI; PYROCOCCUS; PYROCOCCUS SP.;

ALPHA-AMYLASES; CLONING, MOLECULAR; ESCHERICHIA COLI; GENE EXPRESSION; KINETICS; MALTOSE; MOLECULAR WEIGHT; PYROCOCCUS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 84896706820     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-5068-6     Document Type: Article

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