Inverted sugar syrup attained from sucrose hydrolysis using a membrane reactor

Tomotani, Ester Junko; Vítolo, Michele

doi:10.1590/s1984-82502010000300022

Cited by 12 publications

(11 citation statements)

References 9 publications

(17 reference statements)

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“…Reports suggested B. cereus TA‐11 showed β‐ d ‐fructofuranosidase activity optimum at 50°C, but found to have retained only 50% enzyme activity for 20 min (Yoon et al, ). The applicability of B. subtilis β‐ d ‐fructofuranosidase can be advantageous in the food industries for the production of invert sugar syrups which is carried out at 30°C–45°C (Tomotani & Vitolo, ).…”

Section: Discussionmentioning

confidence: 99%

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Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Lincoln

Reddy

2018

J Food Biochem

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The purification and biochemical characterization of extracellular β‐d‐fructofuranosidase from Bacillus subtilis LYN12 was carried out. The enzyme was purified 6.94 folds over the crude extract by gel filtration chromatography with recovery of 15.58%. The molecular mass of ∼66 kDa estimated by SDS‐PAGE was confirmed by LC‐MS as 64512.31 Da. Bacterial β‐d‐fructofuranosidase was found to be a glycoprotein with 62.64% carbohydrate content, and exhibited enhanced activities at broad pH, temperature and stable at pH 7.0, 40°C, respectively. The enzyme showed high affinity for d‐sucrose. Kinetic parameters Km and Vmax were 41.98 mM and 1.184 µmol/min, respectively. β‐d‐fructofuranosidase activity was inhibited by the divalent metal ions Cu2+ and Hg2+, whereas improved by Mg2+, Fe2+ and few sulphydryl group reagents. β‐d‐fructofuranosidase demonstrated ethanol tolerance up to 15% with 76.4% of activity. B. subtilis LYN12 invertase is suggested as a potential enzyme with suitable characteristics for numerous industrial applications. Practical applications β‐d‐fructofuranosidases are one of the industrially important carbohydrases utilized in many applications such as beverages, baking, confectionaries, nutraceuticals and also medicinal formulations. The production of β‐d‐fructofuranosidase from Bacillus subtilis LYN12 by solid‐state fermentation demonstrates the utilization of agro‐industrial wastes, such as wheat bran and molasses. The bacterial β‐d‐fructofuranosidase was produced extracellularly which aids in down‐streaming processes. Most of the industrial alcohol fermentations generally operate at 10%–14% (v/v) of ethanol at the end of fermentation. Interestingly, β‐d‐fructofuranosidase exhibited a significant tolerance towards ethanol, the tolerance level of the bacterial invertase indicates its potentiality in the alcoholic fermentation processes. On the other hand, B. subtilis LYN12 β‐d‐fructofuranosidase was found to be active at a broad pH and temperature range possessing high affinity for d‐sucrose. The biochemical characterization of the bacterial β‐d‐fructofuranosidase is crucial to understand the enzymic nature and properties.

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Section: Discussionmentioning

confidence: 99%

“…The applicability of B. subtilis β-d-fructofuranosidase can be advantageous in the food industries for the production of invert sugar syrups which is carried out at 30°C-45°C (Tomotani & Vitolo, 2010).…”

Section: Discussionmentioning

confidence: 99%

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Lincoln

Reddy

2018

J Food Biochem

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“…The enzyme produced by A. niveus was fully stable at 40–50°C in agreement with the data on most of the known fungal β‐ d ‐fructofuranosidases, which are stable in a temperature range from 30 to 50°C (Said & Pietro, ). The enzymatic production of invert sugar in food industry has been performed at 30–45°C, showing advantages on the acid hydrolysis such as absence of undesirable by‐products (Tomotani & Vitolo, ). The thermal stability observed for the enzyme produced by A. niveus is in agreement with the industrial protocol.…”

Section: Discussionmentioning

confidence: 99%

Characterization of an extracellular β-d -fructofuranosidase produced by Aspergillus niveus during solid-state fermentation (SSF) of cassava husk

2017

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Here, Aspergillus niveus produced an extracellular b-D-fructofuranosidase during SSF of cassava husk. This enzyme was purified 8.5-fold (recovery of 5.2%). A 37-kDa protein band was observed after 8% SDS-PAGE. Native molecular mass is 91.2 kDa. Optimal temperature and pH of activity were 558C and 4.5, respectively. The enzyme was stable at 508C for 1 hr, and 80% of its activity was retained after 1 hr at pH 8.0. The enzymatic activity was improved by Mn Practical applicationsb-D-Fructofuranosidase is an enzyme that can be applied to different industrial sectors, especially food and beverage industries. It is responsible for the hydrolysis of sucrose and yields an equimolar mixture of D-glucose and D-fructose, named as inverted sugar syrup, with broad applications in the confectionery industry. The Aspergillus niveus enzyme hydrolyzed only sucrose here and can be considered a true invertase, showing its potential for application to invert sugar production.Besides, the use of cassava husk for enzyme production means an interesting utilization route of this agroindustrial residue. Thus, characterization of this enzyme is an important step for identification of its potential for practical applications. Cassava (Manihot esculenta Crantz) is an important source of food in different tropical countries such as those located in Asia, Africa, and Latin America (Lateef & Ojo, 2016;Zhang et al., 2016). The main part of this plant is the root, which has 62% moisture content, 1.3% of fiber, 1.1% of liquid waste, and 34% of carbohydrates (Prado, Martins, Alcalde, Zeoula, & Marques, 2000). As for its carbohydrate composition, cassava root contains up to 90% starch in terms of dry weight (Zhang et al., 2016). The residues generated from the cassava processing can be classified into four groups: peels from initial processing, fibrous byproducts, starch residues, and wastewater effluents; the solid residues from cassava and flour processing are termed bagasse (Ubalua, 2007;Zhang et al., 2016) | M AT ER I AL S A N D M E TH ODS | The microorganism and culture conditionsThe filamentous fungus A. niveus, stored in the culture collection of the Laboratory of Microbiology of Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, University of São Paulo, was maintained in PDA (potato-dextrose-agar) slants at 48C until use. New cultures were started by scraping 30-day-old cultures, and the spores were inoculated into PDA slants preautoclaved for 15 min at 1208C and 1.5 atm.SSF was conducted using different agroindustrial residues or products (sugar cane bagasse, corncob, cassava husk, oatmeal, rye flour, wheat bran, or barley bagasse) as a substrate humidified with tap water (1:1 wt/vol), and preautoclaved at 1208C and 1.5 atm for 15 min. Sugar cane bagasse, cassava husk, and barley bagasse were dried before hand at 608C for 48 hr. After that, 10 g of a solid substrate was inoculated with 1 mL of a spore suspension (10 5 spores/mL) to obtain the concentration of 10 4 spores/g of substrate, and the mixture was incubated at 308C for...

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“…Despite acidic sucrose hydrolysis being viable for obtaining syrup, the enzymatic process is preferable being a mild reaction (4.5 < pH < 5.0 and 30 o C < T < 50 o C) (Vitolo, 2004). Moreover, there is no undesirable byproduct formation (Tomotani, Vitolo, 2010). Invertase was chosen for this study because it is inexpensive and abundantly available.…”

Section: Introductionmentioning

confidence: 99%

Sucrose hydrolysis by invertase using a membrane reactor: effect of membrane cut-off on enzyme performance

Addezio

Yoriyaz

Cantarella

et al. 2014

Braz. J. Pharm. Sci.

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Sucrose hydrolysis by invertase [EC.3.2.1.26] produces inverted sugar syrup, an ingredient mainly used in the food industry. To properly catalyze hydrolysis, the enzyme should be reused after this reaction. It is advisable to maintain constant activity over a considerable period. Thus, sucrose hydrolysis was performed in a membrane bioreactor -a continuously stirred tank reactor coupled with an ultrafiltration membrane (UFM) which provides good diffusion and high activity per unit volume. Molecular weight cut-off for soluble invertase UFMs was up to 100kDa. This study focused on the role of UFM invertase cut-off as it is the main element in the process. We demonstrated that both the cut-off and chemical nature of the UFM affected specific invertase activity. Uniterms:Invertase. Membrane Reactor.Sucrose/hydrolysis.A hidrólise da sacarose através da invertase [EC.3.2.1.26] gera xarope de açúcar invertido, que é usado principalmente como ingrediente na indústria alimentícia. Para ter-se uma hidrólise satisfatória, a enzima deve ser reaproveitada após a reação. É desejável que sua atividade seja mantida constante durante um período considerável de reação. A hidrólise da sacarose foi realizada em um reator com membrana (RM) -que é um reator continuamente agitado acoplado a uma membrana de ultrafiltração (MUF) -, porque apresenta efeitos mínimos de difusão e elevada atividade por unidade de volume. O corte molecular da MUF utilizada para reter a invertase solúvel dentro do MR foi de até 100kDa. Como a invertase é o elemento principal deste processo, este trabalho foi focado no papel do corte molecular da MUF na sua atividade. O corte molecular e a natureza química da membrana-UF mostraram afetar a atividade específica da invertase.Unitermos: Invertase. Reator de Membrana. Sacarose/hidrólise.

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Inverted sugar syrup attained from sucrose hydrolysis using a membrane reactor

Cited by 12 publications

References 9 publications

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Characterization of an extracellular β-d -fructofuranosidase produced by Aspergillus niveus during solid-state fermentation (SSF) of cassava husk

Sucrose hydrolysis by invertase using a membrane reactor: effect of membrane cut-off on enzyme performance

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