A bacterial strain, BIT-B35T, was isolated from the gut of plastic-eating larvae of the Coleoptera insect Zophobas atratus. Its taxonomic position was determined by using a polyphasic approach. Cells were white-pigmented, Gram-stain-negative, motile short rods with terminal flagella. The 16S rRNA gene sequence (1411 bp) of strain BIT-B35T showed highest similarity (98.1%) to Escherichia fergusonii ATCC 35469T and Citrobacter koseri LMG 5519T. The results of phylogenetic analyses, based on the 16S rRNA gene, concatenated sequences of seven housekeeping genes (atpD, gyrB, infB, rpoB, pyrG, fusA and leuS) and genome sequences, placed strain BIT-B35T in a separate lineage among the family of Enterobacteriaceae . The major fatty acids were C16 : 0, C17 : 0 cyclo and C19 : 0 cyclo ω8c. The genomic DNA G+C content of strain BIT-B35T was 57.1 mol%. The chemotaxonomic data plus results of physiological and biochemical tests also distinguished strain BIT-B35T from members of other genera within the family Enterobacteriaceae . Therefore, strain BIT-B35T is considered to represent a novel species of a novel genus within the family Enterobacteriaceae , for which the name Intestinirhabdus alba gen. nov., sp. nov. is proposed. The type strain is BIT-B35T (=CGMCC 1.17042T=KCTC 72448T).

Cutinases(3.1.1.74) are serine esterases that belong to the α/β hydrolase family. Such enzymes are usually produced by phytopathogenic microorganisms in order to penetrate their hosts. Cutinase can degrade the stratum corneum in the leaves or the keratin of the cork in the bark. Cutinase hydrolyzes soluble esters, insoluble triglycerides and various polyesters. In addition to the hydrolysis reaction, cutinase also shows synthetic activity and transester activity. Therefore, as a multifunctional enzyme, cutinase has many fields of application. In recent years, it has been found that cutinase can biodegrade plastic and biomoodifie synthetic fibers. Cutinase is the most important enzyme in solving plastic pollution.