Immobilization of malto‐oligosaccharide forming α‐amylase from <i>Bacillus subtilis</i> KCC103: properties and application in starch hydrolysis

Rajagopalan, Gobinath; Krishnan, Chandraraj

doi:10.1002/jctb.1922

Cited by 21 publications

(14 citation statements)

References 20 publications

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“…But the immobilized enzyme offered the advantage of using the enzyme in repeated batch reactions. Immobilized beads prepared from 3% (w/v) alginate and 4% (w/v) CaCl 2 were suitable for up to 10 repeated uses, losing only 25% of their efficiency (Rajagopalan & Krishnan, 2008). It was observed that a-amylase covalently immobilized onto phthaloyl chloride-containing amino group functionalized glass beads demonstrated more than 98% activity after six runs (Kahraman, Bayramoglu, Kayaman-Apohan, & Gungor, 2007b).…”

Section: Reactor Studies Using Immobilized Beadsmentioning

confidence: 97%

“…The above features would be important in the development of an economically feasible bioreactor for the starch hydrolysis industry thus immobilizing a-amylase would be of great importance. The general methods employed for immobilization are entrapment, microencapsulation, copolymerization, cross linking, physical adsorption, chemical attachment and covalent binding (Hasirci, Aksoy, & Tumturk, 2006;Markweghanke, Lang, & Wagner, 1995;Mozhaev et al, 1989;Rajagopalan & Krishnan, 2008;Reshmi, Sanjay, & Sugunan, 2006). Immobilization by physical adsorption on inorganic materials such as porous silica (Cao, Bornscheuer, & Schmid, 1999) clay (Sanjay & Sugunan, 2005a, 2005b and collagen (Groom, Meising, & White, 1988) has been reported.…”

Section: Introductionmentioning

confidence: 97%

“…The gelation characteristics can be altered easily thus capsule characteristics such as the thickness or permeability to different substrates of the gel membrane can be easily controlled (Bladino, Macias, & Cantero, 2002). Alginate beads have been successfully used for the entrapment of a-amylase of Bacillus subtillus and effectively used for starch hydrolysis ( Rajagopalan & Krishnan, 2008). The present study has exploited the simple technique of 0963-9969/$ -see front matter Ó 2009 Elsevier Ltd. All rights reserved.…”

Section: Introductionmentioning

confidence: 98%

See 2 more Smart Citations

Immobilized bacterial α-amylase for effective hydrolysis of raw and soluble starch

Gangadharan

Nampoothiri

Sivaramakrishnan

et al. 2009

Food Research International

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Section: Reactor Studies Using Immobilized Beadsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 98%

See 1 more Smart Citation

Immobilized bacterial α-amylase for effective hydrolysis of raw and soluble starch

Gangadharan

Nampoothiri

Sivaramakrishnan

et al. 2009

Food Research International

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“…For food‐industry applications, calcium alginate gels have been investigated due to their compatibility in many food matrices for a variety of enzymes, including cheese ripening enzymes, glucose isomerase, and β‐ d ‐galactosidase . That said, there has been limited investigation into the efficacy of alginate as an entrapment matrix for ɑ‐amylase, whose substrate (starch, a polymer of ɑ‐1,4 linked glucose monomers) is substantially larger than the aforementioned enzymes . With proper supplementation of the alginate with silica gel, improved immobilization efficiency, and reusability was observed with the immobilized enzyme compared to without added silica.…”

Section: Other Proposed Strategiesmentioning

confidence: 99%

Recent advances in immobilization strategies for glycosidases

Karav

Cohen

Barile

et al. 2016

Biotechnology Progress

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Glycans play important biological roles in cell-to-cell interactions, protection against pathogens, as well as in proper protein folding and stability, and are thus interesting targets for scientists. Although their mechanisms of action have been widely investigated and hypothesized, their biological functions are not well understood due to the lack of deglycosylation methods for large-scale isolation of these compounds. Isolation of glycans in their native state is crucial for the investigation of their biological functions. However, current enzymatic and chemical deglycosylation techniques require harsh pretreatment and reaction conditions (high temperature and use of detergents) that hinder the isolation of native glycan structures. Indeed, the recent isolation of new endoglycosidases that are able to cleave a wider variety of linkages and efficiently hydrolyze native proteins has opened up the opportunity to elucidate the biological roles of a higher variety of glycans in their native state. As an example, our research group recently isolated a novel Endo-β-N-acetylglucosaminidase from Bifidobacterium longum subsp. infantis ATCC 15697 (EndoBI-1) that cleaves N-N′-diacetyl chitobiose moieties found in the N-linked glycan (N-glycan) core of high mannose, hybrid, and complex N-glycans. This enzyme is also active on native proteins, which enables native glycan isolation, a key advantage when evaluating their biological activities. Efficient, stable, and economically viable enzymatic release of N-glycans requires the selection of appropriate immobilization strategies. In this review, we discuss the state-of-the-art of various immobilization techniques (physical adsorption, covalent binding, aggregation, and entrapment) for glycosidases, as well as their potential substrates and matrices.

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“…Thus, immobilization is an important tool for the stability and frequent use of enzymes in industrial application and for its rapid separation from the reaction mixture. Immobilization of the enzyme can be achieved in one of the following ways like entrapement, coplymerization, microencapsulation, cross-linking, covalent binding, chemical attachment and physical adsorption (Hasicri, Aksoy, and Tumturk, 2006;Rajagopalan and Krishnan, 2008;Reshmi, Sanjay and Sugnan, 2006). As a result, the above features are important for the development of economically feasible bioreactor.…”

Section: Review Articlementioning

confidence: 99%

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

Sachdev

Ojha

Mishra

2016

Int J Appl Sci Biotechnol

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Amylase is one of the leading enzymes used in industry from decades. The preliminary function of this enzyme is the hydrolysis of the starch molecule into glucose units and oligosaccharides. Amylases have spectacular application in broad spectrum of industries such as food, detergent, pharmaceutical and fermentation industries. Among different type of amylases α-amylase is in utmost demand because of its striking features. This particular enzyme is a good substitute over the chemicals catalyst used in industries. α-amylases can be acquired from different sources such as microorganism, animals and plants. Microorganisms are the major source of production of amylase because of the ease of availability, manipulation and operation. The starch converting enzymes is basically generated using submerged fermentation. Some of the prominent characteristics of amylase are its mode of action, substrate specificity and operating condition (temperature and pH). Amylases from different bacterial sources contribute differently to the particular trait of the enzyme. Bacillus amylases have been studied and applied so far because of their robustness in nature and easy accessible pure form of it. Thus this makes it more specific and fit for distinct application in the industry. The purpose of this manuscript was the comparative analysis of the physical and chemical features of α amylases from Bacillus species. It also focuses on the unique characteristics of this enzyme and their industrial applications.

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Immobilization of malto‐oligosaccharide forming α‐amylase from Bacillus subtilis KCC103: properties and application in starch hydrolysis

Cited by 21 publications

References 20 publications

Immobilized bacterial α-amylase for effective hydrolysis of raw and soluble starch

Immobilized bacterial α-amylase for effective hydrolysis of raw and soluble starch

Recent advances in immobilization strategies for glycosidases

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

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