TY - JOUR
T1 - Cellotriose-hydrolyzing activity conferred by truncating the carbohydrate-binding modules of Cel5 from Hahella chejuensis
AU - Lee, Hee Jin
AU - Kim, In Jung
AU - Youn, Hak Jin
AU - Yun, Eun Ju
AU - Choi, In Geol
AU - Kim, Kyoung Heon
N1 - Funding Information:
This work was supported by a grant from the National Research Foundation of Korea (2013M1A2A2072597). IJK acknowledges grant support from Korea University. This study was performed at the Korea University Food Safety Hall for the Institute of Biomedical Science and Food Safety.
PY - 2017/2
Y1 - 2017/2
N2 - Processivity is a typical characteristic of cellobiohydrolases (CBHs); it enables the enzyme to successively hydrolyze the ends of cellulose chains and to produce cellobiose as the major product. Some microbes, which do not have CBHs, utilize endoglucanases (EGs) that exhibit processivity, commonly referred to as processive EGs. A processive EG identified from Hahella chejuensis, HcCel5, has a catalytic domain (CD) belonging to the glycoside hydrolase family 5 (GH5) and two carbohydrate-binding modules (CBM6s). In this study, we compared HcCel5-CD with the CD of Saccharophagus degradans Cel5H (SdCel5H-CD), which is a processive EG reported previously. Our results showed that in comparison to SdCel5H-CD, HcCel5-CD has more suitable characteristics for cellulose hydrolysis, such as higher hydrolytic activity, thermostability (40–80 °C), and processivity. Noticeably, HcCel5-CD is capable of hydrolyzing cellotriose, unlike HcCel5. These features of HcCel5-CD for cellulose hydrolysis could be employed for efficient saccharification of lignocellulose to produce cellobiose and glucose, which may be used to produce renewable fuels and chemicals.
AB - Processivity is a typical characteristic of cellobiohydrolases (CBHs); it enables the enzyme to successively hydrolyze the ends of cellulose chains and to produce cellobiose as the major product. Some microbes, which do not have CBHs, utilize endoglucanases (EGs) that exhibit processivity, commonly referred to as processive EGs. A processive EG identified from Hahella chejuensis, HcCel5, has a catalytic domain (CD) belonging to the glycoside hydrolase family 5 (GH5) and two carbohydrate-binding modules (CBM6s). In this study, we compared HcCel5-CD with the CD of Saccharophagus degradans Cel5H (SdCel5H-CD), which is a processive EG reported previously. Our results showed that in comparison to SdCel5H-CD, HcCel5-CD has more suitable characteristics for cellulose hydrolysis, such as higher hydrolytic activity, thermostability (40–80 °C), and processivity. Noticeably, HcCel5-CD is capable of hydrolyzing cellotriose, unlike HcCel5. These features of HcCel5-CD for cellulose hydrolysis could be employed for efficient saccharification of lignocellulose to produce cellobiose and glucose, which may be used to produce renewable fuels and chemicals.
KW - Cel5
KW - Cellulase
KW - Hahella chejuensis
KW - Processive endoglucanase
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U2 - 10.1007/s00449-016-1692-8
DO - 10.1007/s00449-016-1692-8
M3 - Article
C2 - 27761654
AN - SCOPUS:84991761822
VL - 40
SP - 241
EP - 249
JO - Bioprocess and Biosystems Engineering
JF - Bioprocess and Biosystems Engineering
SN - 1615-7591
IS - 2
ER -