Cloning, expression and characterization of a novel fructosyltransferase from <i>Aspergillus niger</i> and its application in the synthesis of fructooligosaccharides

Mao, Shuhong; Liu, Yanna; Yang, Juanjuan; Ma, Xiaoyu; Zeng, Fang; Zhang, Zhaohui; Wang, Shan; Han, Hai‐Chao; Qin, Hao; Lu, Fuping

doi:10.1039/c9ra02520k

Cited by 14 publications

(12 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The sweetness effect and viscous texture of fructooligosaccharides encourage their application in the food industry [82]. Fructosyltransferase production was widely reported from the Aspergillus genus, including Aspergillus oryzae [84], Aspergillus niger [85], Aspergillus aculeatus [86]. However, [82] reported applying Aureobasidium pullulans for fructosyltransferase commercial production.…”

Section: Transferases (Ec 2)mentioning

confidence: 99%

A Comprehensive Insight into Fungal Enzymes: Structure, Classification, and Their Role in Mankind’s Challenges

El‐Gendi

Saleh

Badierah

et al. 2021

JoF

View full text Add to dashboard Cite

Enzymes have played a crucial role in mankind’s challenges to use different types of biological systems for a diversity of applications. They are proteins that break down and convert complicated compounds to produce simple products. Fungal enzymes are compatible, efficient, and proper products for many uses in medicinal requests, industrial processing, bioremediation purposes, and agricultural applications. Fungal enzymes have appropriate stability to give manufactured products suitable shelf life, affordable cost, and approved demands. Fungal enzymes have been used from ancient times to today in many industries, including baking, brewing, cheese making, antibiotics production, and commodities manufacturing, such as linen and leather. Furthermore, they also are used in other fields such as paper production, detergent, the textile industry, and in drinks and food technology in products manufacturing ranging from tea and coffee to fruit juice and wine. Recently, fungi have been used for the production of more than 50% of the needed enzymes. Fungi can produce different types of enzymes extracellularly, which gives a great chance for producing in large amounts with low cost and easy viability in purified forms using simple purification methods. In the present review, a comprehensive trial has been advanced to elaborate on the different types and structures of fungal enzymes as well as the current status of the uses of fungal enzymes in various applications.

show abstract

Section: Transferases (Ec 2)mentioning

confidence: 99%

A Comprehensive Insight into Fungal Enzymes: Structure, Classification, and Their Role in Mankind’s Challenges

El‐Gendi

Saleh

Badierah

et al. 2021

JoF

View full text Add to dashboard Cite

show abstract

“…XOBP48 and found that the specific activity for sucrose was 1219.17 U/mg. 29 Mao et al reported that the specific activity of purified FTase from A. niger TCCC41686 was 6448.92 U/ mg. 30 Our study first indicates that residue site 43 in the catalytic pocket is important for the activity of FruSG, and the replacement of Cys43 by Asn can significantly enhance the specific activity of FruSG (Figure 2B/C).…”

Section: ■ Results and Discussionmentioning

confidence: 62%

“…Moreover, the relative activities (percentage) of FruSG or its mutants were obtained by making a comparison with the highest activity of the same enzyme at other temperatures. The thermal stabilities of FruSG and its mutants were determined by incubating enzymes at different temperatures (30,40,50,60, and 70 °C) in Mcllvaine buffer (100 mmol/L, pH 5.5) for 2 h. After incubation, FruSG activities were measured at 45 °C in Mcllvaine buffer (100 mmol/L, pH 5.5). For one enzyme, the residual activities of FruSG or its mutants after 2 h of incubation at 30 °C were taken as 100%.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Significant Improvement of Both Catalytic Efficiency and Stability of Fructosyltransferase from Aspergillus niger by Structure-Guided Engineering of Key Residues in the Conserved Sequence of the Catalytic Domain

Xia

Guo

Han

et al. 2022

J. Agric. Food Chem.

View full text Add to dashboard Cite

Fructosyltransferase is a key enzyme in fructo-oligosaccharide production, while the highly demanding conditions of industrial processes may reduce its stability and activity. This study employs sequence alignment and structural analysis to target three potential residues (Gln38, Ile39, and Cys43) around the active center of FruSG from Aspergillus niger, and mutants with greatly improved activity and stability were obtained through site-directed mutagenesis. The K m values of C43N and Q38Y were, respectively, reduced to 60.8 and 93.1% compared to those of WT. Meanwhile, the k cat of C43N was increased by 21.2-fold compared to that of WT. These imply that both the affinity and catalytic efficiency of C43N were significantly enhanced compared to WT. The Glide docking score of sucrose inside C43N was calculated to be −5.980, which was lower than that of WT (−4.887). What is more, the proposed general acid/base catalyst Glu273 with a lower pK a value of C43N calculated by PROPKA might contribute to an easier catalytic reaction compared to that of WT. The thermal stability and pH stability of the mutant C43N were significantly enhanced compared to those of WT, and more hydrogen bonds formed during molecular dynamics simulations might contribute to the improved stability of C43N.

show abstract

“…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%

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

View full text Add to dashboard Cite

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.

show abstract

Cloning, expression and characterization of a novel fructosyltransferase from Aspergillus niger and its application in the synthesis of fructooligosaccharides

Abstract: Fructosyltransferases have been used in the industrial production of fructooligosaccharides (FOS).

Cited by 14 publications

References 37 publications

A Comprehensive Insight into Fungal Enzymes: Structure, Classification, and Their Role in Mankind’s Challenges

A Comprehensive Insight into Fungal Enzymes: Structure, Classification, and Their Role in Mankind’s Challenges

Significant Improvement of Both Catalytic Efficiency and Stability of Fructosyltransferase from Aspergillus niger by Structure-Guided Engineering of Key Residues in the Conserved Sequence of the Catalytic Domain

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

Contact Info

Product

Resources

About