A novel thermophilic endoglucanase (EGt) was extracted from a mesophilic fungus (Fusarium oxysporum L19). We invoked conventional kinetic enzyme reactions using the sodium salt of carboxymethyl cellulose (CMC-Na) as substrate. EGt displayed optimal activity at 75℃ when kept running 30 min in the temperature range of 30―85℃. Thermal stability curve measured at 70℃ suggested that its half-life time is 15.1 min. The activity was enhanced in the presence of Co2+ or Mg2+ but inhibited by Pb2+ and Fe3+. Moreover, N-bromosuccinimide (NBS) modification resulted in a complete loss of EGt activity, suggesting that tryptophan residues 5 be involved in the enzyme active site. Amino acid composition analysis demonstrated that EGt contains more proline residues. EGt lacks activity towards p-nitrophenyl cellobiose (pNPC). The N-terminal amino acid sequence of EGt is SYRVPAANGFPNP- DASQEKQ, and the gene of EGt was sequenced and analyzed. Extensive sequence alignments failed to show any homology between EGt and any known endoglucanases. This is the first report addressing the thermal adaptation of a cellulolytic enzyme from the mesophilic fungus F. oxysporum. 5be the expression of multiple isoenzyme in an organism helps it adapt to complex living environments.