Immobilization of lipase using hydrophilic polymers in the form of hydrogel beads.

Hydrolysis of sucrose by invertase immobilized onto novel magnetic polyvinylalcohol microspheres

The invention relates to a process of fermenting plant material in a fermentation medium into a fermentation product using a fermenting organism, wherein one or more carbonic anhydrases are present in the fermentation medium.

Processes for producing fermentation products

Immobilization of a thermostable α-amylase onto reactive membranes: kinetics characterization and application to continuous starch hydrolysis

https://www.researchgate.net/file.PostFileLoader.html?id=554b337ed2fd64d94b8b4571&assetKey=AS%3A273772341334022%401442283820753

Immobilization of invertase within calcium alginate gel capsules

A solution of 10 g/L of sodium alginate (Satialgine® types used [Sanofi trademark]: SG800® and S1100® with manuronic/guluronic ratio of 0.5 and 1.2, respectively) containing invertase (0.08 g of protein/L) was dropped into 0.1 M CaCl2 solution buffered at pH 4.0, 7.0, or 8.0. The beads were left to harden in CaCl2 solution for 24 h. The high immobilization yield of 60% occurred with SG800 at pH8.0. The activity of soluble and insoluble invertase was measured against pH (2.8–8.0), sucrose concentration (4.5–45 mM), and temperature (30–60°C). Both forms presented an optimum pH of 4.6. However, the soluble invertase was stable at the overall pH interval studied, whereas insoluble invertase lost 30% of its original activity at pH > 5.0. At temperatures above 40°C, the insoluble form was more stable than the soluble one. The kinetic constants and activation energies (E
 a
 ) for free invertase were K
 M
 =41.2 mM, V
 max=0.10 mg of TRS/(min · mL), and E
 a
 28 kJ/mol for entrapped invertase they were (K
 M
 )
 ap
 =7.2 mM, (V
 max)
 ap
 =0.060 mg of TRS/(min · mL), and (E
 a
 )ap=24 kJ/mol.

L. M. O. Arruda

Papers

Characterization of invertase entrapped into calcium alginate beads.