Harnessing -arabinose isomerase for biological production of -tagatose: Recent advances and its applications

Ravikumar, Yuvaraj; Ponpandian, Lakshmi Narayanan; Zhang, Guoyan; Yun, Jimmy; Qi, Xianghui

doi:10.1016/j.tifs.2020.11.020

Cited by 42 publications

(24 citation statements)

References 149 publications

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“…With 100 g/L D-galactose as the substrate at pH 8.0°C and 60°C, about 33% of D-galactose was converted by TMAI at 16 h, and slowly reached 37% at 24 h (Figure 1d). These results indicated that TMAI was the limiting step for D-tagatose production, which was consistent with the previous reports (Ravikumar et al, 2021).…”

Section: Enzymatic Properties Of β-Galactosidase and L-arabinose Isom...supporting

confidence: 93%

“…It is well known that the industrial enzymatic process is always limited to the catalytic efficiency and thermostability, especially for multistep bioconversion. Researchers have been characterizing and engineering different L‐arabinose isomerases from various bacteria, which indeed show better catalytic efficiency and thermo‐stability (Ravikumar et al, 2021). Alternatively, enzyme immobilization could also be another effective approach (DiCosimo et al, 2013; Fernandez‐Lafuente, 2019; Ravikumar et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

“…Researchers have been characterizing and engineering different L‐arabinose isomerases from various bacteria, which indeed show better catalytic efficiency and thermo‐stability (Ravikumar et al, 2021). Alternatively, enzyme immobilization could also be another effective approach (DiCosimo et al, 2013; Fernandez‐Lafuente, 2019; Ravikumar et al, 2021). To improve the catalytic efficiency of the multistep bioconversion process, biological cascade catalysis has become a promising tool, which is widely used for the synthesis of various value‐added chemicals (Ko & Lee, 2018; X. Luo et al, 2019; You et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Self‐assembling protein scaffold‐mediated enzymes' immobilization enhances in vitrod‐tagatose production from lactose

Liu

Jiang

Zhang

et al. 2022

Food Bioengineering

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As a rare low-calorie sugar with special medicinal value, D-tagatose is widely used in the field of food, beverages, medicine, and cosmetics. However, enzymatic D-tagatose production in vitro is commonly limited to low conversion efficiency and poor thermo-stability. Herein, taking advantage of the self-assembling property of protein scaffold EutM (ethanolamine bacterial microcompartments), Spy and Snoop peptide pairs was used to drive the linkage between the EutM and cargo proteins, βgalactosidase (BagB), and L-arabinose isomerase (TMAI) to construct a dual-enzymes cascade and realize the D-tagatose production from lactose. The optimal conditions of the cascade were shown to be pH of 8.0, temperature of 60°C, 100 g/L lactose as substrate with supplementing 5 mM Mn 2+ . When the ratio of immobilized enzymes to EutM scaffold reached 1:6, the D-tagatose productivity of the dual-enzymes cascade could reach 1.03 g/L/h, which was 1.24-fold higher than free enzymes. In addition, the EutM-based scaffold could efficiently improve the stability of immobilized enzymes, in which 45% of the activity remained after 12 h, 2.14-fold higher than the free one. Overall, an attractive EutM-based selfassembling platform immobilizing BagB and TMAI was developed, showing enhanced catalysis efficiency and enzyme thermo-stability for D-tagatose production.

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Section: Enzymatic Properties Of β-Galactosidase and L-arabinose Isom...supporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Self‐assembling protein scaffold‐mediated enzymes' immobilization enhances in vitrod‐tagatose production from lactose

Liu

Jiang

Zhang

et al. 2022

Food Bioengineering

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“…A major breakthrough was the discovery that the enzyme arabinose isomerase (EC 5.3.1.4) that catalyzes the reversible isomerization of arabinose into ribulose could also catalyze the isomerization of galactose into tagatose, although with a lower affinity and reactivity for galactose than for arabinose [68]. Therefore, considerable effort has been made in the last decade to engineer this enzyme for tagatose production [69], including genetic engineering [70], protein engineering [71] and biocatalyst engineering strategies [72], both with isolated arabinose isomerase [72] and whole-cells containing it [73]. The industrial production of tagatose considers lactose hydrolysis, either chemically with mineral acids or enzymatically with β-galactosidase, followed by isomerization with arabinose isomerase [74].…”

Section: Other Lactose-derived Health Promoting Bioactive Compoundsmentioning

confidence: 99%

Trends in lactose-derived bioactives: synthesis and purification

Vera

Guerrero

Illanes

2022

Syst Microbiol and Biomanuf

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Lactose obtained from cheese whey is a low value commodity despite its great potential as raw material for the production of bioactive compounds. Among them, prebiotics stand out as valuable ingredients to be added to food matrices to build up functional foods, which currently represent the most active sector within the food industry. Functional foods market has been growing steadily in the recent decades along with the increasing awareness of the World population about healthy nutrition, and this is having a strong impact on lactose-derived bioactives. Most of them are produced by enzyme biocatalysis because of molecular precision and environmental sustainability considerations. The current status and outlook of the production of lactose-derived bioactive compounds is presented with special emphasis on downstream operations which are critical because of the rather modest lactose conversion and product yields that are attainable. Even though some of these products have already an established market, there are still several challenges referring to the need of developing better catalysts and more cost-effective downstream operations for delivering high quality products at affordable prices. This technological push is expected to broaden the spectrum of lactose-derived bioactive compounds to be produced at industrial scale in the near future.

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“…However, some harmful effects, including the negative effects on intestinal microbial composition, have made them unattractive as the sugar substitutes. In contrast, rare sugars and polyols like D -psicose, D -tagatose, and D -arabitol, have been shown to have health bene ts, making them attractive to researchers and food industries (Felipe Hernández-Pérez et al 2019;Ravikumar et al 2021). Belonging to a pentitol family, D -arabitol (C 5 H 12 O 5 , M.wt 152) has a caloric value (0.2 kcal/g) much lower than sucrose (4 kcal/g), which is present naturally in low quantities in yeast, lichens, mushroom, and higher fungi (Kordowska-Wiater 2015).…”

Section: Introductionmentioning

confidence: 99%

Enhanced Biosynthesis of D-Arabitol by Metschnikowia reukaufii Through Optimizing Medium Composition and Fermentation Conditions

Huang

Zabed

et al. 2022

Appl Biochem Biotechnol

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D -arabitol is an important functional sugar alcohol, which can be used in the preparation of foods, chemicals, and medicines. Despite biological production of D -arabitol from low-cost substrates has recently been the focus of research, low yield of this technology has limited its large-scale exploitation.Optimization of this bioprocess could be a promising option to improve the yield of D -arabitol. In this study, one-factor-at-a-time (OFAT) strategy and Box-Behnken design (BBD) were used to increase Darabitol production by Metschnikowia reukau i CICC 31858 through optimizing the fermentation conditions and medium composition. The OFAT optimization provided the optimal conditions for temperature, agitation speed, and fermentation time of 30℃, 220 rpm, and 144 h, respectively. Likewise, the optimum concentrations of peptone, ammonium sulfate, KH 2 PO 4 , MgSO 4 •7H 2 O, and fumaric acid in the fermentation medium were (g/L) 7.5, 1, 2 , 0.5 and 7.5, respectively. Under these optimum conditions, 80.43 g/L of D -arabitol was produced from 200 g/L of glucose, with a productivity of 0.56 g/L/h. The BBD optimization with three important components of fermentation medium (KH 2 PO 4 , MgSO 4 •7H 2 O and fumaric acid) showed that the predicted titer of D -arabitol varied from 47.21 g/L to 89.27 g/L, and the actual titer of D -arabitol ranged from 47.36 to 89.83 g/L. The optimum concentrations (g/L) of KH 2 PO 4 , MgSO 4 •7H 2 O, and fumaric acid in the fermentation medium were found to be 1.0, 0.5, and 4.7g/L, respectively. Under the optimum conditions, 92.45 g/L of D -arabitol was nally produced with the yield and productivity of 0.46 g/g and 0.64 g/L/h, respectively.

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Harnessing -arabinose isomerase for biological production of -tagatose: Recent advances and its applications

Cited by 42 publications

References 149 publications

Self‐assembling protein scaffold‐mediated enzymes' immobilization enhances in vitrod‐tagatose production from lactose

Self‐assembling protein scaffold‐mediated enzymes' immobilization enhances in vitrod‐tagatose production from lactose

Trends in lactose-derived bioactives: synthesis and purification

Enhanced Biosynthesis of D-Arabitol by Metschnikowia reukaufii Through Optimizing Medium Composition and Fermentation Conditions

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