fig1 is a cross - sectional view showing one example of a support with enzyme immobilized thereon . referring to fig1 numeral 1 is an enzyme - immobilizing support , and numeral 2 is a layer including the enzyme . the uneven surface of the immobilizing support 1 is covered in advance with enzyme or an enzyme - containing layer 2 . then , when the immobilizing reagent acts thereupon , the immobilization can be performed with the shape as it is being maintained . thus , the adhesion between the support and the immobilizing enzyme membrane is also better . on the other hand , as a method of decreasing the decline of the enzyme activity caused through immobilization , the immobilizing reagent is supplied under conditions where the enzyme substrate or coenzyme in the enzyme requiring the coenzyme are coexistent with the enzyme . this is based on assumption that the coexistence of the enzyme substrate or the coenzyme stabilizes the structure of the enzyme . it is difficult to apply this method to a conventional method for immobilization of enzyme , which supplies the immobilizing reagent from the above - described liquid phase . however , in the method for immobilization of enzyme in accordance with the present invention , the immobilizing operation can be easily performed even when the enzyme substrate or the coenzyme are coexistent . namely , the immobilizing support is covered with a layer including the enzyme and at least the enzyme substrate or the coenzyme in the enzyme requiring the coenzyme . then , the immobilizing reaction is performed while the immobilizing reagent is being supplied from the vapor phase thereby to decrease the decline in enzyme activity caused by the immobilizing reaction for the immobilizing operation . as a method of causing the enzyme to coexist with the enzyme substrate or the coenzyme , they , together with the enzyme , are placed in solution and thereafter the surface of support for immobilizing enzyme is coated . also , the coexistence can be provided under vapor conditions in a case of the substrate having high vapor pressure such as ethanol or the like in alcohol dehydrogenase . the several examples of the present invention are presented as follows . fig2 is a cross - sectional view showing an example wherein enzyme 4 is immobilized , by the method of the present invention , to the lower end portion of a glass electrode 3 . the ion - selective membrane of the lower end of the glass electrode 3 is coated with immobilized urease . the producing method is as follows . the urease is used as enzyme 4 . the urease is mixed with bovine serum albumin to form a dilute solution . thereafter , the ion selective portion of the glass electrode 3 is covered with it by a spreading method , etc . then , after some drying operation , the immobilizing reaction is performed for 60 minutes at 25 ° c . in glutaraldehyde vapor , so that the sufficiently adhesive immobilized - enzyme membrane is provided . after the reaction completion , it is rinsed in phosphate buffer solution . according the measurements of variation in electrode potential with respect to urea concentration , in tris buffer solution by the electrode , a superior straight - line relationship was obtained with respect to the logarithmic plot of the urea concentration of 1 × 10 - 2 to 1 × 10 - 4 mole / l as shown in fig3 . fig4 shows the relationship between the immobilizing reaction time and the electrode potential with respect to the urea concentration 2 × 10 - 3 mole / l . as apparent from fig4 it is found out that sufficient immobilization is performed because of approximately 60 minutes &# 39 ; immobilizing reaction within the example 1 . glass beads are filled into a glass column . then , a dilute solution of α - amylase , as the enzyme flows into the column . thereafter , air is fed through the column for a drying operation , and the glutaraldehyde vapor is fed at 25 ° c . for approximately 60 minutes to perform the immobilizing reaction . after the reaction , water is fed for a rinsing operation , so that an α - amylase immobilized column is provided . fig5 is a cross - sectional view showing the immobilized column in connection with an example 2 of the present invention . referring to fig5 numeral 5 is a glass column , numeral 6 shows glass beads filling the inside of the column 5 , numeral 7 shows enzyme immobilized on the column inner wall and the glass bead surface and numeral 8 shows space portions among the enzyme 7 . it was found , in example 2that when starch solution , as substrate , in phosphate buffer solution , ph5 , was supplied to this column to provide maltose , a sufficient enzyme activity was maintained . in addition , superior properties were provided such as a decrease in the enzyme activity decline caused due to the continuous use , or the like . fig6 is a cross - sectional view showing one example wherein enzyme is immobilized by the method of the present invention on the surface of a nesa - glass electrode to constitute an enzyme electrode for measurement of substrate concentration . referring to fig6 numeral 7 is a glass layer , numeral 10 is nesa - layer , numeral 11 is an ag - paste layer for electric contact and numeral 12 is an epoxy resin layer for insulation . the surface of nesa - layer is coated with immobilized alcohol dehydrogenase 13 . the manufacturing method of the enzyme electrode according to an example 3 of the present invention is as follows . phosphate buffer solution wherein alcohol dehydrogenase is dissolved ( 100 mg / ml ), and phosphate buffer solution wherein nicotinamide adenine dinucleotide ( nad ) as coenzyme is dissolved ( 100 mg / ml ) are mixed , at the volume ratio of 3 : 1 with respect to each other . the mixed solution is spread on the surface of the above - described nesa - glass electrode . then , after a drying operation , the immobilizing reaction is performed , in the glutaraldehyde vapor , at 25 ° c . for 60 minutes . after the reaction , it is rinsed with the phosphate buffer solution . the immobilized enzyme membrane thus provided was sufficient in adhesive property . this enzyme electrode is referred to as a . also , an enzyme electrode was made , under conditions the wherein the coenzyme and the substrate coexist , as described hereinafter . the mixed solution of the enzyme and the coenzyme is applied and spread on the surface of the nesa - glass and is dried as described hereinabove . then , ethanol is used as the substrate . in the vapor of the ethanol and the glutaraldehyde , the immobilizing reaction is performed at 25 ° c . for 60 minutes and thereafter it is rinsed . the electrode thus provided is referred to as b . for comparison with the electrodes a and b , the nesa - glass surface was coated with the enzyme solution only and thereafter the immobilizing reaction was performed in the glutaraldehyde vapor by such a method as described hereinabove . the electrode is referred to as c . the ethanol concentration is measured , by a method as described hereinafter , with the above - described alcohol dehydrogenase immobilized electrode . the above - described electrode is immersed in the phosphate buffer solution , ph7 . 0 , containing the nad of 1 × 10 - 3 mole / l as the coenzyme . the electrode is set to a constant potential of 0 . 4 volts vs . a saturated calomel electrode using a potentiostat , and thereafter the ethanol was added to a given concentration . the anodic current of the coenzyme is measured . the current shows a steady state value in about one minute after the pouring of the ethanol . fig7 shows the relationship between ethanol concentration and the current increase portion in connection with the example 3 . the electrodes a and b provided by the immobilizing method of the present invention are larger in current increase as compared with the electrode c provided by the immobilizing reaction under a condition where the coenzyme and the substrate do not coexist . this is because the enzyme activity decline accompanied by the immobilization is descreased by the coexistence of coenzyme or substrate . as described hereinabove , according to the method for immobilization of enzyme in accordance with the present invention , the enzyme can be immobilized extremely easily on various supports without chemical modifications . also , after the immobilizing reaction has been performed on the glass plate or the like by the present method , reaction products are peeled off to easily provide an immobilized enzyme membrane . the immobilizing reagent usable according to the method of the present invention is not restricted to glutaraldehyde employed in the examples . polymerized aldehydes or aldehydes such as 2 - hydroxyadipaldehyde crotonaldehyde , acrolein , glyoxal , propionaldehyde , paraformaldehyde could be used . also , when the surface of the immobilizing support is coated in advance with enzyme , a macromolecular substance which forms the covalent bond through reaction with the immobilizing reagent is mixed with the enzyme and is used , so that the immobilizing operation becomes easier and the enzyme activity decline can be reduced . in addition , the strength of the immobilized enzyme membrane can be increased . macromolecular substances such as polyethylenimine , polyornithine , polylysine , polyargine , albumin , etc . desirably have functional groups represented by - nh 2 ,& gt ; nh , - sh . the mutual bonds among enzymes , between enzyme and the macromolecular substances or among macromolecular substances advance due to the reaction between these functional groups and the immobilizing reagents , and the reaction between the enzymes and the immobilizing reagents . also , when the functional groups exist on the surface of the immobilizing support , a covalent bond can be formed between the support surface and the enzyme and be immobilized by the method of the present invention . although the present invention has been described and illustrated in detail , it is to be clearly understood that the same is by way of limitation , the spirit and scope of the present invention being limited only by the terms of the appended claims .