Microbial invertases: A review on kinetics, thermodynamics, physiochemical properties

Nadeem, Habibullah; Rashid, Muhammad Hamid; Siddique, Muhammad Hussnain; Azeem, Farrukh; Muzammil, Saima; Javed, Muhammad Rizwan; Ali, Muhammad Amjad; Rasul, Ijaz; Riaz, Muhammad

doi:10.1016/j.procbio.2015.04.015

Cited by 75 publications

(62 citation statements)

References 82 publications

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“…The production of bacterial β‐ d ‐fructofuranosidases is commonly by submerged fermentation conditions (Lincoln & More, ; Nadeem et al, ). Some studies have demonstrated enhancement of invertase production by optimization strategies.…”

Section: Discussionmentioning

confidence: 99%

“…The hydrolytic activity and β‐ d ‐fructofuranosidase regulation has been researched systematically mostly in yeasts (Linde et al, ; Oliveira et al, ; Sainz‐Polo et al, ). Many food industries extensively utilize the popular yeast strain Saccharomyces cerevisiae as a potent β‐ d ‐fructofuranosidase producer, since these strains are regarded to be nonpathogenic, nontoxicogenic and approved by the Food and Drug Administration (FDA) (Nadeem et al, ). However, several Bacillus species possess great prospects in industries and are generally regarded as safe.…”

Section: Introductionmentioning

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%

Section: Introductionmentioning

confidence: 99%

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Lincoln

Reddy

2018

J Food Biochem

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“…Inverted sugar is sweeter than sucrose and do not crystallizes. Because of these properties it is widely used in food industry for the production of jams, candies, and soft‐centered chocolates (Nadeem et al, ). Sucrose can also be hydrolyzed by acid solution.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of an invertase and a transfructosylase from Aspergillus terreus

et al. 2018

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Two intracellular invertases from Aspergillus terreus were purified and characterized. Invertase 1 has been shown maximal activity at pH 3.0 and optimum temperature at 60°C, while invertase 2 presented maximal activity at pH 4.6 and optimum temperature at 55°C. Km of invertase 1 and 2 for sucrose were 9.8 and 6.2 mM, respectively. Invertase 2 showed high thermostability presenting half‐life of 44, 14.9, and 2 hr at 40, 55, and 60°C, respectively. Gel filtration and SDS‐PAGE analysis revealed that invertase 2 has a dimeric structure composed by two monomers of 32 kDa. Fructose was a competitive inhibitor for invertase 2 presenting Ki of 61.5 mM. Besides hydrolytic activity, invertase 2 also showed transfructosylating activity producing fructooligosaccharides. The enzymes have potential to be applied in food industry since its product, inverted sugar, is used in candies and syrup production, while fructooligosacharides are prebiotics, low calorie and noncariogenic sweeteners. Practical applications Enzymes invertases hydrolyze sucrose in glucose and fructose producing inverted sugar. This product is widely used in food industry to produce jams, syrups, and fondant fillings for chocolates. Besides hydrolysis activity, some invertases can also present transfructosylating activity producing fructooligosaccharides. These oligosaccharides can act as prebiotic, providing beneficial health effects and can be used as low calorie and noncariogenic sweeteners. Aspergillus terreus produced two intracellular enzymes, one exclusively invertase, and the other, invertase and transfructosylase. The enzymes were purified and characterized in this study. This is an important step on screening new enzymes able to produce inverted sugar and fructooligosaccharides from sucrose.

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“…Acid invertases have been the most extensively studied and isolated from various sources while much less is known about alkaline invertases which have been reported only from plants and cyanobacteria2452021222324.…”

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confidence: 99%

Characterization of a novel low-temperature-active, alkaline and sucrose-tolerant invertase

Zhou

Gao

et al. 2016

Sci Rep

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A glycoside hydrolase family 32 invertase from Bacillus sp. HJ14 was expressed in Escherichia coli. The purified recombinant enzyme (rInvHJ14) showed typical biochemical properties of low-temperature-active and alkaline enzymes: (i) rInvHJ14 was active and stable in the range of pH 7.0–9.5 with an apparent pH optimum of 8.0; (ii) rInvHJ14 was most active but not stable at 30–32.5 °C, with 19.7, 48.2 and 82.1% of its maximum activity when assayed at 0, 10 and 20 °C, respectively, and the Ea, ΔG* (30 °C), Km (30 °C) and kcat (30 °C) values for hydrolysis of sucrose by rInvHJ14 was 47.6 kJ mol−1, 57.6 kJ mol−1, 62.9 mM and 746.2 s−1, respectively. The enzyme also showed strong sucrose tolerance. rInvHJ14 preserved approximately 50% of its highest activity in the presence of 2045.0 mM sucrose. Furthermore, potential factors for low-temperature-active and alkaline adaptations of rInvHJ14 were presumed. Compared with more thermostable homologs, rInvHJ14 has a higher frequency of glycine residues and a longer loop but a lower frequency of proline residues (especially in a loop) in the catalytic domain. The catalytic pockets of acid invertases were almost negatively charged while that of alkaline rInvHJ14 was mostly positively charged.

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Microbial invertases: A review on kinetics, thermodynamics, physiochemical properties

Cited by 75 publications

References 82 publications

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Purification and characterization of an invertase and a transfructosylase from Aspergillus terreus

Characterization of a novel low-temperature-active, alkaline and sucrose-tolerant invertase

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