Entrapment of <svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-0.2811508pt" id="M1" height="8.47856pt" version="1.1" viewBox="-0.0657574 -8.19741 10.3275 8.47856" width="10.3275pt"><g transform="matrix(.018,0,0,-0.018,0,0)"><path id="g113-223" d="M545 106L524 126C493 85 467 65 455 65C438 65 427 113 405 238C448 295 498 362 543 439L533 448L478 435C453 386 423 331 398 295H395C370 404 347 448 282 448C169 448 23 309 23 153C23 54 65 -12 128 -12C203 -12 283 70 339 155H341C360 29 380 -12 411 -12C444 -12 491 11 545 106ZM333 204C265 95 210 54 169 54C137 54 113 96 113 171C113 302 191 405 252 405C301 405 318 306 333 204Z"/></g></svg>-Amylase in Agar Beads for Biocatalysis of Macromolecular Substrate

<table>Thermal inactivation kinetics of free and entrapped <i>α</i>-amylase. (a) Free enzyme; (b) <i>α</i>-amylase entrapped in agar gel; (c) <i>α</i>-amylase entrapped in ionotropically complexed calcium agar hydrogel; and (d) Arrhenius plots for free and entrapped enzyme.</table>

International Scholarly Research Notices

fig5

Figure 5

Figure 5: Entrapment of <svg xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg" style="vertical-align:-0.2811508pt" id="M1" height="8.47856pt" version="1.1" viewBox="-0.0657574 -8.19741 10.3275 8.47856" width="10.3275pt"><g transform="matrix(.018,0,0,-0.018,0,0)"><path id="g113-223" d="M545 106L524 126C493 85 467 65 455 65C438 65 427 113 405 238C448 295 498 362 543 439L533 448L478 435C453 386 423 331 398 295H395C370 404 347 448 282 448C169 448 23 309 23 153C23 54 65 -12 128 -12C203 -12 283 70 339 155H341C360 29 380 -12 411 -12C444 -12 491 11 545 106ZM333 204C265 95 210 54 169 54C137 54 113 96 113 171C113 302 191 405 252 405C301 405 318 306 333 204Z"/></g></svg>-Amylase in Agar Beads for Biocatalysis of Macromolecular Substrate 

International Scholarly Research Notices

Entrapment of -Amylase in Agar Beads for Biocatalysis of Macromolecular Substrate

Figure 5