Title : Enhancing PET hydrolytic enzyme activity by fusion of the cellulose-binding domain of cellobiohydrolase I from Trichoderma reesei - Dai_2021_J.Biotechnol_334_47 |
Author(s) : Dai L , Qu Y , Huang JW , Hu Y , Hu H , Li S , Chen CC , Guo RT |
Ref : J Biotechnol , 334 :47 , 2021 |
Abstract :
The large amounts of polyethylene terephthalate (PET) that enter and accumulate in the environment have posed a serious threat to global ecosystems and human health. A PET hydrolase from PET-assimilating bacterium Ideonella sakaiensis (IsPETase) that exhibits superior PET hydrolytic activity at mild conditions is attracting enormous attention in development of plastic biodegrading strategies. In order to enhance the PET hydrolysis capacity of IsPETase, we selected several polymer-binding domains that can adhere to a hydrophobic polymer surface and fused these to a previously engineered IsPETase(S121E/D186H/R280A) (IsPETase(EHA)) variant. We found that fusing a cellulose-binding domain (CBM) of cellobiohydrolase I from Trichoderma reesei onto the C-terminus of IsPETase(EHA) showed a stimulatory effect on enzymatic hydrolysis of PET. Compared to the parental enzyme, IsPETase(EHA)_CBM exhibited 71.5 % and 44.5 % higher hydrolytic activity at 30 degC and 40 degC, respectively. The catalytic activity of IsPETase(EHA)_CBM was increased by 86 % when the protein concentration was increased from 2.5 microg/mL to 20microg/mL. These findings suggest that the fusion of polymer-binding module to IsPETase is a promising strategy to stimulate the enzymatic hydrolysis of PET. |
PubMedSearch : Dai_2021_J.Biotechnol_334_47 |
PubMedID: 34044062 |
Gene_locus related to this paper: idesa-peth |
Gene_locus | idesa-peth |
Family | Polyesterase-lipase-cutinase |
Dai L, Qu Y, Huang JW, Hu Y, Hu H, Li S, Chen CC, Guo RT (2021)
Enhancing PET hydrolytic enzyme activity by fusion of the cellulose-binding domain of cellobiohydrolase I from Trichoderma reesei
J Biotechnol
334 :47
Dai L, Qu Y, Huang JW, Hu Y, Hu H, Li S, Chen CC, Guo RT (2021)
J Biotechnol
334 :47