Co-immobilization of dextransucrase and dextranase in alginate

Ölçer, Zehra; Tanrıseven, Aziz

doi:10.1016/j.procbio.2010.06.011

Cited by 39 publications

(13 citation statements)

References 22 publications

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“…The glucose produced due to the saccharifying enzyme in SST process is not allowed to accumulate as it will be concurrently transglucosylated by ␣-glucosidase to produce oligosaccharides thereby lowering the possible inhibition caused by liberated glucose. The combined use of two such enzymes for the IMO production was also reported elsewhere where IMO and oligo dextrans were synthesized from sucrose using the enzymes dextransucrase and dextranase, which is different from the current study [15][16][17].…”

Section: Introductionmentioning

confidence: 60%

“…In their process dextransucrase was used to convert sucrose into dextran with fructose as a by-product, whereas the obtained dextran was further converted to IMO by dextranase. Dextransucrase from and dextranase were also co-immobilized in alginate and used to produce isomaltooligosaccharides from sucrose [17]. Nevertheless, this process is not identical to SST, as their enzymes do not carry saccharification.…”

Section: Time Course Studies Of Sst In Batch Experimentsmentioning

confidence: 99%

See 1 more Smart Citation

Production of isomaltooligosaccharides (IMO) using simultaneous saccharification and transglucosylation from starch and sustainable sources

Basu

Mutturi

Prapulla

2016

Process Biochemistry

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Section: Introductionmentioning

confidence: 60%

Section: Time Course Studies Of Sst In Batch Experimentsmentioning

confidence: 99%

Production of isomaltooligosaccharides (IMO) using simultaneous saccharification and transglucosylation from starch and sustainable sources

Basu

Mutturi

Prapulla

2016

Process Biochemistry

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“…Thermostability studies of immobilized pectinase revealed that it retained >80% of its initial activity after 5 d storage at 30°C while its free form retained only 30% of initial activity [ 24 ]. Coimmobilization in the alginate fibers and beads also resulted in protein leaching and decreased enzymatic activity after one month storage at 4°C [ 10 ]. Barbosa et al [ 25 ] opined that thermal stabilizations of lipase-B at different pH values are consequences of both intramolecular chemical modification and intermolecular cross-linking which create the least damaging local environment.…”

Section: Resultsmentioning

confidence: 99%

Improved Enzyme Catalytic Characteristics upon Glutaraldehyde Cross-Linking of Alginate Entrapped Xylanase Isolated fromAspergillus flavusMTCC 9390

2015

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Purified fungal xylanase was entrapped in alginate beads. Its further cross-linking using glutaraldehyde resulted in large enzyme aggregates which may function as both a catalyst and a support material for numerous substrate molecules. Enzyme cross-linking presented a negative impact on enzyme leaching during repeated washings and recovery of enzyme activity was substantial after twelve cycles of usage. The entrapment followed by cross-linking doubled the total bound activity and also greatly improved the enzyme stability at extreme chemical environment. The wide pH stability, better thermo- and storage stability, lowered K m value, and protection from some metal ions are salient achievements of present immobilization. The study shows the efficacy, durability, and sustainability of immobilized catalytic system which could be efficiently used for various juice processing operations.

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“…A previous research showed that enzymes were co-immobilized by encapsulating soluble dextransucrase and dextranase covalently attached in alginate. The alginate capsule resulted in a high immobilization yield (71%), and enzymatic activities were without any decrease after a month in storage at 4 • C (Ölçer & Tanriseven, 2010). This suggests that encapsulation enhances the stability of those enzymes for industrial-scale production.…”

Section: Discussionmentioning

confidence: 90%

Anti-Streptococcus mutans and anti-biofilm activities of dextranase and its encapsulation in alginate beads for application in toothpaste

Juntarachot

Sirilun

Kantachote

et al. 2020

PeerJ

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Background The accumulation of plaque causes oral diseases. Dental plaque is formed on teeth surfaces by oral bacterial pathogens, particularly Streptococcus mutans, in the oral cavity. Dextranase is one of the enzymes involved in antiplaque accumulation as it can prevent dental caries by the degradation of dextran, which is a component of plaque biofilm. This led to the idea of creating toothpaste containing dextranase for preventing oral diseases. However, the dextranase enzyme must be stable in the product; therefore, encapsulation is an attractive way to increase the stability of this enzyme. Methods The activity of food-grade fungal dextranase was measured on the basis of increasing ratio of reducing sugar concentration, determined by the reaction with 3, 5-dinitrosalicylic acid reagent. The efficiency of the dextranase enzyme was investigated based on its minimal inhibitory concentration (MIC) against biofilm formation by S. mutans ATCC 25175. Box-Behnken design (BBD) was used to study the three factors affecting encapsulation: pH, calcium chloride concentration, and sodium alginate concentration. Encapsulation efficiency (% EE) and the activity of dextranase enzyme trapped in alginate beads were determined. Then, the encapsulated dextranase in alginate beads was added to toothpaste base, and the stability of the enzyme was examined. Finally, sensory test and safety evaluation of toothpaste containing encapsulated dextranase were done. Results The highest activity of the dextranase enzyme was 4401.71 unit/g at a pH of 6 and 37 °C. The dextranase at its MIC (4.5 unit/g) showed strong inhibition against the growth of S. mutans. This enzyme at 1/2 MIC also showed a remarkable decrease in biofilm formation by S. mutans. The most effective condition of dextranase encapsulation was at a pH of 7, 20% w/v calcium chloride and 0.85% w/v sodium alginate. Toothpaste containing encapsulated dextranase alginate beads produced under suitable condition was stable after 3 months of storage, while the sensory test of the product was accepted at level 3 (like slightly), and it was safe. Conclusion This research achieved an alternative health product for oral care by formulating toothpaste with dextranase encapsulated in effective alginate beads to act against cariogenic bacteria, like S. mutants, by preventing dental plaque.

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Co-immobilization of dextransucrase and dextranase in alginate

Cited by 39 publications

References 22 publications

Production of isomaltooligosaccharides (IMO) using simultaneous saccharification and transglucosylation from starch and sustainable sources

Production of isomaltooligosaccharides (IMO) using simultaneous saccharification and transglucosylation from starch and sustainable sources

Improved Enzyme Catalytic Characteristics upon Glutaraldehyde Cross-Linking of Alginate Entrapped Xylanase Isolated fromAspergillus flavusMTCC 9390

Anti-Streptococcus mutans and anti-biofilm activities of dextranase and its encapsulation in alginate beads for application in toothpaste

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