A novel thermostable and efficient Class II glucose isomerase from the thermophilic Caldicoprobacter algeriensis: Biochemical characterization, molecular investigation, and application in High Fructose Syrup production

Neifar, Sawssan; Hlima, Hajer Ben; Mhiri, Sonia; Mezghani, Monia; Bouacem, Khelifa; Ibrahim, Adel Hadj; Jaouadi, Bassem; Bouanane‐Darenfed, Amel; Béjar, Samír

doi:10.1016/j.ijbiomac.2019.01.150

Cited by 19 publications

(16 citation statements)

References 44 publications

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“…The optimum temperature for most GIs is between 60°C and 90°C. For example, the optimum temperature of a class II GI from the thermophilic Caldicoprobacter algeriensis was 90°C [13], GI from Thermobifida fusca WSH03-11 is expressed in E. coli with an optimum temperature of 80°C [6]. The optimum temperature of CbGI was higher than that from T. thermosulfurigenes (65°C) [14].…”

Section: Enzymatic Properties Of Purified Recombinant Cbgimentioning

confidence: 99%

“…Also, by gene mining, the optimum temperature for GI from Thermus oshimai is as high as 95°C [7]. It has been reported that, theoretically, 55% conversion can be achieved when the isomerization temperature is above 85°C [13,16]. Although the optimum temperature for many GIs is above 90°C, excessive temperatures for production consume energy and increase production costs [6].…”

Section: Biomed Research Internationalmentioning

confidence: 99%

“…The other thermophilic GIs were reported to obtain high bioconversion rate at high temperature. Such as the maximal bioconversion rate of 54.7% was accomplished by GICA from C. algeriensis at 85°C for 3 h [13], which 52.2% was achieved by TnapXI from T. naphthophila RKU-10 [21].…”

Section: Conversion Efficiency Of Cbgimentioning

confidence: 99%

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A Novel Glucose Isomerase fromCaldicellulosiruptor besciiwith Great Potentials in the Production of High-Fructose Corn Syrup

Dai

Miao

Jiang

et al. 2020

BioMed Research International

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Glucose isomerase (GI) that catalyzes the conversion of D-glucose to D-fructose is one of the most important industrial enzymes for the production of high-fructose corn syrup (HFCS). In this study, a novel GI (CbGI) was cloned from Caldicellulosiruptor bescii and expressed in Escherichia coli. The purified recombinant CbGI (rCbGI) showed neutral and thermophilic properties. It had optimal activities at pH 7.0 and 80°C and retained stability at 85°C. In comparison with other reported GIs, rCbGI exhibited higher substrate affinity (Km=42.61 mM) and greater conversion efficiency (up to 57.3% with 3M D-glucose as the substrate). The high catalytic efficiency and affinity of this CbGI is much valuable for the cost-effective production of HFCS.

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Section: Enzymatic Properties Of Purified Recombinant Cbgimentioning

confidence: 99%

Section: Biomed Research Internationalmentioning

confidence: 99%

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A Novel Glucose Isomerase fromCaldicellulosiruptor besciiwith Great Potentials in the Production of High-Fructose Corn Syrup

Dai

Miao

Jiang

et al. 2020

BioMed Research International

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“…HFS can be divided into three categories according to fructose content: HFS-90 (90% fructose and 10% glucose), HFS-55 (55% fructose and 45% glucose), and HFS-42 (42% fructose and 58% glucose). In general, HFS-55 is more suitable for industrial applications than HFS-42 it has better flavor, sweetness, and other benefits (Fatourehchi et al, 2014;Neifar et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Identification and Immobilization of an Invertase With High Specific Activity and Sucrose Tolerance Ability of Gongronella sp. w5 for High Fructose Syrup Preparation

et al. 2020

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Invertases catalyze the hydrolysis of sucrose into fructose and glucose and can be employed as an alternative in producing high fructose syrup. In this study, we reported the heterologous expression of an invertase gene (GspInv) of Gongronella sp. w5 in Komagataella pastoris. GspInv activity reached 147.6 ± 0.4 U/mL after 5 days of methanol induction. GspInv is invertase with a high specific activity of 2,776.1 ± 124.2 U/mg toward sucrose. GspInv showed high tolerance to sucrose (IC 50 = 1.2 M), glucose (IC 50 > 2 M), fructose (IC 50 = 1.5 M), and a variety of metal ions that make it an ideal candidate for high fructose syrup production. A carbohydratebinding module was sequence-optimized and fused to the N-terminus of GspInv. The fusion protein had the highest immobilization efficiency at room temperature within 1 h adsorption, with 1 g of cellulose absorption up to 8,000 U protein. The celluloseimmobilized fusion protein retained the unique properties of GspInv. When applied in high fructose syrup preparation by using 1 M sucrose as the substrate, the sucrose conversion efficiency of the fused protein remained at approximately 95% after 50 h of continuous hydrolysis on a packed bed reactor. The fused protein can also hydrolyze completely the sucrose in sugarcane molasses. Our results suggest that GspInv is an unusual invertase and a promising candidate for high fructose syrup preparation.

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“…For instance, since the thermodynamic equilibrium of glucose to fructose isomerization increases towards fructose with increasing temperature, xylose isomerase variants with high thermal resistance are desirable. Besides searching for a thermostable natural enzyme with a reasonable activity [92,93], it is also possible to increase the thermostability of an enzyme that already has high activity [94][95][96]. In order to prevent enzyme denaturation induced by glycation (covalent linkage formation between lysine residues and the substrate glucose) as well as encouraged by the notion that the Arg/Lys ratio is higher in thermostable proteins, Mrabet et al substituted some lysines to arginines in XI from Actinoplanes missouriensis [95].…”

Section: Rational Enzyme Engineeringmentioning

confidence: 99%

Xylose isomerase from Piromyces: Characterization and engineering for improving S. cerevisiae-based lignocellulosic bioethanol production

Lee¹

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Xylose isomerases are tetrameric metalloenzymes that catalyze aldoseketose interconversion. Their activity is widely used in industrial biocatalysis, especially for the preparation of high-fructose syrups from glucose-containing starch hydrolysates. The activity with xylose is industrially relevant because it converts xylose that cannot be fermented by yeast to xylulose, which is accepted as a substrate for alcoholic fermentation. Several crystal structures of xylose isomerases have been solved and the catalytic mechanism has been investigated, opening the way to engineering more efficient variants of these enzymes. The properties of xylose isomerases and the potential of protein engineering to improve xylose metabolism by yeast are discussed here.

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A novel thermostable and efficient Class II glucose isomerase from the thermophilic Caldicoprobacter algeriensis: Biochemical characterization, molecular investigation, and application in High Fructose Syrup production

Cited by 19 publications

References 44 publications

A Novel Glucose Isomerase fromCaldicellulosiruptor besciiwith Great Potentials in the Production of High-Fructose Corn Syrup

A Novel Glucose Isomerase fromCaldicellulosiruptor besciiwith Great Potentials in the Production of High-Fructose Corn Syrup

Identification and Immobilization of an Invertase With High Specific Activity and Sucrose Tolerance Ability of Gongronella sp. w5 for High Fructose Syrup Preparation

Xylose isomerase from Piromyces: Characterization and engineering for improving S. cerevisiae-based lignocellulosic bioethanol production

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