Bacterial invertases: Occurrence, production, biochemical characterization, and significance of transfructosylation

Lincoln, Lynette; More, Sunil S.

doi:10.1002/jobm.201700269

Cited by 48 publications

(37 citation statements)

References 68 publications

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“…A yield of 15.58% with purification fold of 6.94 was observed. Similarly, the partial purification by ammonium sulphate precipitation was reported in most studies (Lincoln & More, ), however, solvent precipitation methods by use of acetone or ethanol have not been reported so far. The purification of bacterial invertases by gel filtration was also reported to be a good strategy for high yields as observed in many reports (De Gines et al, ; Warchol et al, ; Yamamoto et al, ; Yoon et al, ).…”

Section: Discussionmentioning

confidence: 86%

“…Bacterial β‐ d ‐fructofuranosidase occurs as both intracellular and extracellular enzymes (Lincoln & More, ). Some of the reported bacterial strains producing extracellular invertases are Arthrobacter globiformis IFO 3062 (Win et al, ), Arthrobacter sp.…”

Section: Discussionmentioning

confidence: 99%

“…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%

“…However, several Bacillus species possess great prospects in industries and are generally regarded as safe. Besides, very few investigations were carried out on β‐ d ‐fructofuranosidases from bacteria which requires attention (Lincoln & More, ).…”

Section: Introductionmentioning

confidence: 99%

“…Majority of the literature emphasizes on invertases from yeasts and moulds, whereas bacteria are the least explored microorganisms. The studies on bacterial β‐ d ‐fructofuranosidases are limited, and very few researchers focus on purification and characterization (Lincoln & More, ). Therefore, it is important to identify newer microbial strains with potential features for β‐ d ‐fructofuranosidase applications.…”

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: 86%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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