In　order　to　investigate　the　mechanism　of　the　different　stimulatory　effects　of　the　biosurfactant　rhamnolipid　and　the　chemical　surfactant　Tween　80　on　enzymatic　hydrolysis　of　lignocellulose,　the　interaction　between　surfactants　and　enzymes　was　analyzed　by　the　fluorescence　probe　method　using　pyrene　as　probe.　Based　on　the　evolution　law　of　pyrene　fluorescence　spectroscopy　in　the　＂surfactants-enzymes＂　systems,　the　interaction　relationship　between　surfactants　and　enzymes　was　analyzed　and　discussed　in　this　paper.　The　results　show　that　enzyme　molecules　bind　with　rhamnolipid　molecules,　participate　in　the　formation　of　rhamnolipid　micelles,　and　increase　the　inner　hydrophobic　polarity　of　micelles,　but　do　not　change　the　properties　of　rhamnolipid　micelles　above　the　CMC　(Critical　Micelle　Concentration).　Nevertheless.　for　Tween　80,　enzyme　molecules　also　participate　in　the　forming　of　micelles.　however,　they　exhibit　a　stronger　interaction　with　enzymes　above　the　CMC.　Both　rhamnolipid　and　Tween　80　bind　more　strongly　with　xylanase　than　cellulase.　Considering　also　previous　experimental　results,　it　can　be　concluded　that　the　interaction　between　surfactants　and　enzymes　improve　enzyme　stability　and　activity,　and,　therefore,　the　efficiency　of　enzymatic　hydrolysis　of　lignocellulose　is　enhanced.　The　findings　further　provide　theoretical　knowledge　about　the　mechanism　of　the　stimulative　effects　of　surfactants　on　enzymatic　hydrolysis　of　lignocellulose.　(C)　2011　Elsevier　Inc.　All　rights　reserved.