Figure 5 shows

Lineweaver-Burk plot for Emulsiflex prepared oxyrase characterized at standard conditions.

Kinetic constants for free and immobilized enzyme were also determined by using the

Lineweaver-Burk plot. The Km values of the free and immobilized enzymes were determined to be 307.7 and 234.2 g/L respectively, while the V max values were determined to be 0.366 g D-Glucose/L.min and 0.415 g D-Glucose/L.min respectively.

These values were determined based on the relationship between 1/[S] with 1/[I.sub.pa]] of the Michaelis-Menten equation and

Lineweaver-Burk plot (Fig.

The enzyme kinetics of recombinant endo-[beta]-1,4-glucanase against CMC-Na was investigated.It revealed that the apparent Km value of the enzyme determined from the

Lineweaver-Burk plot was estimated to be 64.5 mM.

The [V.sub.max] and [K.sub.m] can be obtained by the y-intercept (1/[V.sub.max]) and v-intercept (-1/[K.sub.m]) from a plot of 1/V versus 1/[S] (

Lineweaver-Burk plot).

A

Lineweaver-Burk plot was made by plotting the inverse numbers of the reaction rate V and the concentration of substrate [S]:

The

Lineweaver-Burk plot (Figure 2) was used to calculate the apparent maximum velocity ([V.sub.max]) and Michaelis-Menten constant ([K.sub.m]) for [alpha]-glucosidase activity on maltose in the presence and absence of WEAX.

Competitive, noncompetitive and uncompetitive inhibition can be easily distinguished with the use of double reciprocal plot of the

Lineweaver-Burk plot. Two sets of rate determination in which enzyme concentration was held constant, were carried out.

From linear plots of the Michaelis-Menten equation such as Lineweaver-Burk or Hanes-Woolf plot using an Excel curve fitting program, the [K.sub.m] and [V.sub.max] of recombinant EG1 was calculated: In

Lineweaver-Burk plot ([R.sup.2] = 0.9998) [K.sub.m] and [V.sub.max] were 0.4% CMC and 144.9 U/mg, respectively.

8,9-EET (0.31, 0.47 and 0.63 [micro]M), and several concentrations of the potential inhibitors (0, 0.5, 1,2 and 4 [micro]M for tanshinone IIA, 0, 2.5, 5 and 10 [micro]M for cryptotanshinone, and 0, 5, 10 and 20 [micro]M for salvianolic C) were used for the construction of

Lineweaver-Burk plot and estimation of [K.sub.i] values.

The Michaelis-Menton constant (Km) and the maximum velocity (Vmax) were determined by

Lineweaver-Burk plot.

A

Lineweaver-Burk plot of the data was shown in Figures 7 and 8; Fa-a acted as a noncompetitive inhibitor with the plots of 1/[v] versus 1/[S] gave a family of straight lines with different slopes, which intersected one another in the v-axis [12].