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Guar Gum and Its Derivatives: Pharmaceutical Applications
Published in Amit Kumar Nayak, Md Saquib Hasnain, Dilipkumar Pal, Natural Polymers for Pharmaceutical Applications, 2019
D. Sathya Seeli, M. Prabaharan
The major components of the biosensor are biological responsive component and physical transducer. It converts the biological recognition incident into an appropriate physical signal. In recent years, various types of biopolymers combined with enzyme immobilize electrodes have been reported for the identification of biomolecules (Prabaharan, 2013; Deng et al., 2016). Since the enzyme activity plays a significant role in the performance of biosensors, a great interest is devoted for finding the suitable matrix that can hold the enzymes and retain their biological activities (Kushwah and Bhadauria, 2010). In this respect, the materials based on guar gum have a great scope to be considered as an immobilization matrix for biomolecules due to their desired physicochemical properties. Bagal and Karve (2006) developed the invertase enzyme-immobilized porous membranes based on agarose/guar gum composite and studied their sucrose hydrolytic activity. The immobilization efficacy of invertase enzyme was determined as 91%. Moreover, the activity of invertase was found to be good at pH 4.5–6.5. The enzyme presented the twelve cycles of reusability, improved thermal, and operational stability due to its conformational stability on the surface of the agarose/guar gum matrix. Using a similar approach, Tembe et al., (2006, 2007) developed an agarose/guar gum matrix immobilized with tyrosinase for the identification of micromolar level L-DOPA and dopamine.
EEMS2015 organizing committee
Published in Yeping Wang, Jianhua Zhao, Advances in Energy, Environment and Materials Science, 2018
The catalysis of single enzyme is specific, and dif- ferent enzymes have a fixed effect on one of the soil matrix. Soil enzymes reflect the transforma- tion processes of organic compounds (Guan et al., 1984). A range of previous investigations indi- cated that there is a close relationship between the activities of soil enzyme and the contents of nutrients, because soil enzymes participate in the transformation of nutrients (Paz Jimenez M.D., 2002; Liu, 2011). As shown in Table 3, pH and catalase both have significant positive correla- tion with OM at 0.05 level. Guan et al. found that catalase can destroy the hydrogen peroxide gener- ated by biochemical reactions in soil and reduce the damage to organism (Guan et al., 1984). As a kind of reductase in soil, the activity of catalase characterizes the transformation rate of organic matter (Lv et al., 2009). Invertase and TN have a significant positive correlation at 0.01 level, while TN and HN have a significant positive correla- tion at 0.05 level. Invertase can split sucrose into glucose and fructose. It is clear that invertase can increase the soluble nutrients in the soil. There is
Chemical Kinetics
Published in Franco Battaglia, Thomas F. George, Understanding Molecules, 2018
Franco Battaglia, Thomas F. George
Another example is enzyme catalysis.6 Enzymes are macromolecules (molecular weight of the order of 104–106), remarkable for their effectiveness to catalyze efficiently and selectively many biologically relevant reactions. For instance, the enzyme invertase, produced by some microorganisms (yeasts), catalyzes the hydrolysis reaction of sucrose into glucose and fructose:7
Biochemical characterization and evaluation of invertases produced from Saccharomyces cerevisiae CAT-1 and Rhodotorula mucilaginosa for the production of fructooligosaccharides
Published in Preparative Biochemistry and Biotechnology, 2018
Paula Mirella Gomes Barbosa, Tobias Pereira de Morais, Cinthia Aparecida de Andrade Silva, Flávia Regina da Silva Santos, Nayara Fernanda Lisbo Garcia, G. G. Fonseca, Rodrigo Simões Ribeiro Leite, Marcelo Fossa da Paz
Invertase is able to catalyze sucrose in a mixture containing glucose and fructose, producing invert sugar.[1,2] This enzymatic hydrolysis of sucrose is catalyzed by two types of enzymes: β-d-glucosidase (EC 3.2.1.20) and β-d-fructofuranosidase (EC 3.2.1.26). They carry out the hydrolysis of terminal non-reducing β-fructofuranoside residues to β-fructofuranoside residues. Although invert sugar is formed with both enzymes, only the second one has become known as invertase. These enzymes have different isoforms. Although the specific function of these isoforms remains unknown, they appear to control the entrance of sucrose via different mechanisms.[3] They are found in invertebrates, vertebrates, green algae, bacteria, plants, and fungi.[4]
Immobilization of invertase in calcium alginate and calcium alginate-kappa-carrageenan beads and its application in bioethanol production
Published in Preparative Biochemistry & Biotechnology, 2020
Ishita Malhotra, Seemi Farhat Basir
The enzyme invertase (β-d-fructofuranosidase, E.C. 3.2.1.26) is a glycoprotein which catalyzes the hydrolysis of sucrose producing an equimolar mixture of α-D-glucose and β-D-fructose known as invert syrup. Sucrose can be hydrolyzed either by acid (using hydrochloric acid) or enzyme (using invertase). Enzymatic hydrolysis does not lead to the formation of colored by-products and is environmentally friendly. However, acid hydrolysis is more economical. Moreover, enzymes have been widely accepted as natural catalysts as they possess characteristics like the ease of production, substrate specificity and high sensitivity but their widespread use in industrial applications is often hindered due to lack of long-term operational stability and shelf-storage life, inefficient recovery and reuse making the process noneconomical. Therefore, to match the low cost of acid hydrolysis, the enzyme invertase should be used in an immobilized form.[1] Enzyme immobilization is defined as the process in which the movement of enzyme is restricted in space by attachment to a matrix/support. Immobilization offers various advantages like easy recovery of both enzymes and products from the reaction mixture leading to pure product isolation especially in food and pharmaceutical industries, reuse of enzymes, continuous operation of enzymatic processes, and increased operational stability of enzymes.[2,3] Calcium alginate is a commonly used matrix for the immobilization of invertase by entrapment. Alginate is present in the cell wall of brown algae and is a naturally occurring hydrophilic polysaccharide consisting of (1,4)-linked β-D-mannuronate and α-L-guluronate residues.[4,5] The immobilization of invertase using calcium alginate was studied by various researchers and it has been reported in the literature that more than 80% of the invertase leaked out of the beads.[6] Carrageenan is a sulfated linear polysaccharide consisting of alternate units of D-galactose and 3,6-anhydro-galactose joined by α-1,3 and β-1,4-glycosidic linkage. Kappa-carrageenan has one sulfate group per two galactose molecules and has the property of forming strong and rigid gels. Alginate and kappa-carrageenan, which are polyelectrolytes, can form hydrogels in the presence of divalent cations (Ca+2) through chain pairing leading to efficient encapsulation of enzyme by increasing the mechanical and chemical stability of alginate beads[7,8] overcoming the problem of leakage of enzyme. Based on the literature, a matrix consisting of calcium alginate and kappa-carrageenan was formed for the efficient encapsulation of invertase enzyme in this study. Therefore, the aim of the present study involves the efficient entrapment of invertase in calcium alginate-kappa-carrageenan matrix.