TY - JOUR
T1 - Genetic and Structural Characterization of a Thermo-Tolerant, Cold-Active, and Acidic Endo-β-1,4-glucanase from Antarctic Springtail, Cryptopygus antarcticus
AU - Song, Jung Min
AU - Hong, Seung Kon
AU - An, Young Jun
AU - Kang, Mee Hye
AU - Hong, Kwon Ho
AU - Lee, Youn Ho
AU - Cha, Sun Shin
N1 - Publisher Copyright:
© 2017 American Chemical Society.
PY - 2017/3/1
Y1 - 2017/3/1
N2 - The CaCel gene from Antarctic springtail Cryptopygus antarcticus codes for a cellulase belonging to the glycosyl hydrolase family 45 (GHF45). Phylogenetic, biochemical, and structural analyses revealed that the CaCel gene product (CaCel) is closely related to fungal GHF45 endo-β-1,4-glucanases. The organization of five introns within the open reading frame of the CaCel gene indicates its endogenous origin in the genome of the species, which suggests the horizontal transfer of the gene from fungi to the springtail. CaCel exhibited optimal activity at pH 3.5, retained 80% of its activity at 0-10 °C, and maintained a half-life of 4 h at 70 °C. Based on the structural comparison between CaCel and a fungal homologue, we deduced the structural basis for the unusual characteristics of CaCel. Under acidic conditions at 50 °C, CaCel was effective to digest the green algae (Ulva pertusa), suggesting that it could be exploited for biofuel production from seaweeds.
AB - The CaCel gene from Antarctic springtail Cryptopygus antarcticus codes for a cellulase belonging to the glycosyl hydrolase family 45 (GHF45). Phylogenetic, biochemical, and structural analyses revealed that the CaCel gene product (CaCel) is closely related to fungal GHF45 endo-β-1,4-glucanases. The organization of five introns within the open reading frame of the CaCel gene indicates its endogenous origin in the genome of the species, which suggests the horizontal transfer of the gene from fungi to the springtail. CaCel exhibited optimal activity at pH 3.5, retained 80% of its activity at 0-10 °C, and maintained a half-life of 4 h at 70 °C. Based on the structural comparison between CaCel and a fungal homologue, we deduced the structural basis for the unusual characteristics of CaCel. Under acidic conditions at 50 °C, CaCel was effective to digest the green algae (Ulva pertusa), suggesting that it could be exploited for biofuel production from seaweeds.
KW - Cryptopygus antarcticus
KW - biochemical and structural features
KW - biofuel production from seaweeds
KW - cold-active cellulase
KW - endo-β-1,4-glucanase
KW - horizontal gene transfer
UR - http://www.scopus.com/inward/record.url?scp=85014289602&partnerID=8YFLogxK
U2 - 10.1021/acs.jafc.6b05037
DO - 10.1021/acs.jafc.6b05037
M3 - Article
C2 - 28156112
AN - SCOPUS:85014289602
SN - 0021-8561
VL - 65
SP - 1630
EP - 1640
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 8
ER -