Comparative evaluation of extracellular β‐<scp>d</scp>‐fructofuranosidase in submerged and solid‐state fermentation produced by newly identified<i>Bacillus subtilis</i>strain

Lincoln, Lynette; More, Sunil S.

doi:10.1111/jam.13881

Cited by 8 publications

(6 citation statements)

References 43 publications

(55 reference statements)

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“…β‐ d ‐fructofuranosidase producing bacterium B. subtilis LYN12 (GenBank accession number MF417491.1) identified by 16S rDNA sequencing (Lincoln & More, ) was used in the study. The bacterial isolate was maintained on CDA containing d ‐sucrose as the sole carbon source at pH 5.0.…”

Section: Methodsmentioning

confidence: 99%

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: Methodsmentioning

confidence: 99%

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Lincoln

Reddy

2018

J Food Biochem

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“…[ 22 , 23 , 24 ], Bacillus spp. [ 16 , 19 ], and Bifidobacterium spp. [ 25 ] along with a few other microorganisms, such as Candida spp.…”

Section: Resultsmentioning

confidence: 99%

“…Upon analysis, it was determined that the LcFFase1s protein belongs to the class of typical bacterial β-D-fructofuranosidases. These enzymes typically exhibit molecular weights ranging from 50 kDa to 100 kDa, as exemplified by Bifidobacteriaceae lactis DSM10140T (59.4 kDa) [ 28 ], Bacillus subtilis LYN12 (66 kDa) [ 19 , 29 ], and Microbacterium trichothecenolyticum (approximately 66.2 kDa) [ 3 ]. In contrast, certain fungal β-D-fructofuranosidases display higher protein sizes, such as Aspergillus niger (116 kDa) [ 30 ] and A. oryzae S719 (95 kDa) [ 31 ].…”

Section: Resultsmentioning

confidence: 99%

“…w5 [ 17 ], and Leuconostoc mesenteroides [ 18 ]. Reports on the hydrolysis of stachyose by β-D-fructofuranosidase are even rarer [ 19 ]. Therefore, the discovery of the unique hydrolytic characteristics of LcFFase1s provides a solid foundation for exploring the broader applications of this enzyme in the future.…”

Section: Resultsmentioning

confidence: 99%

“…Yeasts are the primary producers of β-D-fructofuranosidase [ 10 , 11 ] followed by molds [ 12 , 13 , 14 ] and some bacteria [ 15 , 16 ]. However, most of these commonly used microbial β-D-fructofuranosidases are highly efficient in catalyzing sucrose with limited research conducted on their enzymatic activity towards raffinose or stachyose [ 3 , 17 , 18 , 19 ]. To date, only a few β-D-fructofuranosidases have been identified to possess this unique activity, including those from Microbacterium trichothecenolyticum [ 3 ], Bacillus sp.…”

Section: Introductionmentioning

confidence: 99%

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Efficient Degradation for Raffinose and Stachyose of a β-D-Fructofuranosidase and Its New Function to Improve Gel Properties of Coagulated Fermented-Soymilk

Zhou

Shen

Jing

2023

Gels

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A novel β-D-fructofuranosidase gene was identified via database mining from Leptothrix cholodnii. The gene was chemically synthesized and expressed in Escherichia coli, resulting in the production of a highly efficient enzyme known as LcFFase1s. The enzyme exhibited optimal activity at pH 6.5 and a temperature of 50 °C while maintaining stability at pH 5.5–8.0 and a temperature below 50 °C. Furthermore, LcFFase1s exhibited remarkable resistance to commercial proteases and various metal ions that could interfere with its activity. This study also revealed a new hydrolysis function of LcFFase1s, which could completely hydrolyze 2% raffinose and stachyose within 8 h and 24 h, respectively, effectively reducing the flatulence factor in legumes. This discovery expands the potential applications of LcFFase1s. Additionally, the incorporation of LcFFase1s significantly reduced the particle size of coagulated fermented-soymilk gel, resulting in a smoother texture while maintaining the gel hardness and viscosity formed during fermentation. This represents the first report of β-D-fructofuranosidase enhancing coagulated fermented-soymilk gel properties, highlighting promising possibilities for future applications of LcFFase1s. Overall, the exceptional enzymatic properties and unique functions of LcFFase1s render it a valuable tool for numerous applications.

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Microbial Valorization: Strategies for Agro-Industry Waste Minimization and Value-Added Product Generation

Ibarruri

Hernández

2021

Bio-Valorization of Waste

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Comparative evaluation of extracellular β‐d‐fructofuranosidase in submerged and solid‐state fermentation produced by newly identifiedBacillus subtilisstrain

Abstract: Bacillus subtilis LYN12 invertase possesses excellent fermenting capability to utilize agro-industrial residues under submerged and solid-state conditions. This could be a beneficial candidate in food and beverage processing industries.

Cited by 8 publications

References 43 publications

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Purification and biochemical characterization of β-d-fructofuranosidase fromBacillussubtilisLYN12

Efficient Degradation for Raffinose and Stachyose of a β-D-Fructofuranosidase and Its New Function to Improve Gel Properties of Coagulated Fermented-Soymilk

Microbial Valorization: Strategies for Agro-Industry Waste Minimization and Value-Added Product Generation

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