This　study　aimed　to　improve　the　stability　and　catalytic　properties　of　Thermomyces　lanuginosus　lipase　(TLL)　adsorbed　on　a　hydrophobic　support.　At　the　optimized　conditions　(pH　5　and　25　degrees　C　without　any　additions),　the　Sips　isotherm　model　effectively　fitted　the　equilibrium　adsorption　data,　indicating　a　monolayer　and　the　homogenous　distribution　of　immobilized　lipase　molecules.　To　preserve　the　high　specific　activity　of　adsorbed　lipase,　the　immobilized　lipase　(IL)　with　a　moderate　loading　amount　(approximately　40%　surface　coverage)　was　selected.　Polyethylenimine　(PEI)　and　chitosan　(CS)　were　successfully　applied　as　bridging　units　to　in　situ　crosslink　the　immobilized　lipase　molecules　in　IL.　At　the　low　polymer　concentration　(0.5%,　w/w)　and　with　1　h　incubation,　insignificant　changes　in　average　pore　size　were　detected.　Short-chain　PEI　and　CS　(MW　＜=　2　kDa)　efficiently　improved　the　lipase　stability,　i.e.,　the　lipase　loss　decreased　from　40%　to　＜2%.　Notably,　CS　performed　much　better　than　PEI　in　maintaining　lipase　activity.　IL　crosslinked　with　CS-2　kDa　showed　a　two-　to　three-fold　higher　rate　when　hydrolyzing　p-nitrophenyl　butyrate　and　a　two-fold　increase　in　the　catalytic　efficiency　in　the　esterification　of　hexanoic　acid　with　butanol.　These　in　situ　crosslinking　strategies　offer　good　potential　for　modulating　the　catalytic　properties　of　TLL　for　a　specific　reaction.