A novel thermophilic β-glucosidase from Caldicellulosiruptor bescii: Characterization and its synergistic catalysis with other cellulases

Bai, Aixi; Zhao, Xinyu; Jin, Yanwei; Yang, Guangyu; Feng, Yan

doi:10.1016/j.molcatb.2012.09.016

Cited by 23 publications

(9 citation statements)

References 58 publications

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“…β-Glucosidase activity rapidly increased in the initial 18 hr of the fermentation process. Compared to other enzymes, β-glucosidase activity, the rate-limiting factor during the enzymatic hydrolysis of cellulose (Bai, Zhao, Jin, Yang, & Feng, 2013), was generally high. Endoglucanase, a key enzyme for effective cellulose degradation (Xue et al, 2017), disrupts the noncrystalline region of cellulose and randomly hydrolyzes the β-1, 4-glucosidic linkage to degrade the long molecular chains into a smaller molecule fragments with a reducing end.…”

Section: Enzyme Activity Analysis During Wheat Bran Prefermentationmentioning

confidence: 90%

“…As shown in Figure 2a, increase in fermentation time resulted in a small increment in exoglucanase activity, an indication of no restriction by endoglucanase and β-glucosidase. Compared to other enzymes, β-glucosidase activity, the rate-limiting factor during the enzymatic hydrolysis of cellulose (Bai, Zhao, Jin, Yang, & Feng, 2013), was generally high. This might be due to the high content of both endoglucanase and exoglucanase at the start of the prefermentation process which provided sufficient substrate for β-glucosidase.…”

Section: Enzyme Activity Analysis During Wheat Bran Prefermentationmentioning

confidence: 90%

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Use ofKluyveromyces marxianusprefermented wheat bran as a source of enzyme mixture to improve dough performance and bread biochemical properties

et al. 2019

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Background and objectives: In this study, Kluyveromyces marxianus with ability to produce β-glucosidase was used to preferment wheat bran (WB) and release a mixture of natural enzymes for improving dough performance and bread quality.Five different enzyme activities were analyzed. The effect of the prefermented WB with enzyme mixture on stickiness and microstructure of dough, ferulic acid release in bread, and molecular weight distribution of arabinoxylan were evaluated using Texture Analyzer, scanning electron microscopy (SEM), HPLC, and highperformance gel filtration chromatography (HPGFC). Findings: Kluyveromyces marxianus exhibited abundant extracellular β-glucosidase activity (up to 6.98 U/g). The main enzymes released in prefermented bran were endoglucanase and exoglucanase, β-glucosidase, xylanase, and ferulate esterases. These enzymes were active during bread making (only prefermented bran added as improver or combined with xylanase) and affected solubility and molecular weight distribution of dietary fiber, which resulted in positive improvement of dough performance, release of phenolic acid, and overall quality of the breads. The changes observed were attributed to the extracellular enzymes from K. marxianus and endogenous enzymes activated during prefermentation, thus enhancing the WB functionality in bread. Conclusions: Wheat bran bioprocessing using high enzyme producing yeasts increases functional application of wheat bran in baked products. Significance and novelty: This study added new knowledge for developing a natural enzyme-based improver for bran-enriched baked products in the food industry. K E Y W O R D Sdough rheology, Kluyveromyces marxianus, natural enzymes, prefermentation, wheat bran

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Section: Enzyme Activity Analysis During Wheat Bran Prefermentationmentioning

confidence: 90%

Section: Enzyme Activity Analysis During Wheat Bran Prefermentationmentioning

confidence: 90%

Use ofKluyveromyces marxianusprefermented wheat bran as a source of enzyme mixture to improve dough performance and bread biochemical properties

et al. 2019

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“…(2) Ion Exchange Resins. Sulfonic acid functionalities of ion exchange resin with solid acid catalyst and sulfonic acid functioned materials resulted in high yield at 63% and 76% in pure dimethyl sulfoxide (DMSO) solvent, correspondingly [142,143]. Solid acids such as amorphous carbon materials consisting of SO 3 H groups layered transition (HNbMoO 6 ) metal oxide and resin sulfated have been tested for the cellulose hydrolysis, but the yield of glucose is still comparatively less [144,145].…”

Section: Homogeneous Catalystmentioning

confidence: 99%

Functionalized Activated Carbon Derived from Biomass for Photocatalysis Applications Perspective

Bagheri

Julkapli

Hamid

2015

International Journal of Photoenergy

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This review highlighted the developments of safe, effective, economic, and environmental friendly catalytic technologies to transform lignocellulosic biomass into the activated carbon (AC). In the photocatalysis applications, this AC can further be used as a support material. The limits of AC productions raised by energy assumption and product selectivity have been uplifted to develop sustainable carbon of the synthesis process, where catalytic conversion is accounted. The catalytic treatment corresponding to mild condition provided a bulk, mesoporous, and nanostructure AC materials. These characteristics of AC materials are necessary for the low energy and efficient photocatalytic system. Due to the excellent oxidizing characteristics, cheapness, and long-term stability, semiconductor materials have been used immensely in photocatalytic reactors. However, in practical, such conductors lead to problems with the separation steps and loss of photocatalytic activity. Therefore, proper attention has been given to develop supported semiconductor catalysts and certain matrixes of carbon materials such as carbon nanotubes, carbon microspheres, carbon nanofibers, carbon black, and activated carbons have been recently considered and reported. AC has been reported as a potential support in photocatalytic systems because it improves the transfer rate of the interface charge and lowers the recombination rate of holes and electrons.

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“…Research efforts have recently focused on extremely thermophilic microorganisms for exploring novel cellulases and other GHs to improve the current situation [ 5 – 7 ], due to the advantages of these thermophilic enzymes, such as higher reaction velocity, excellent thermostability, and decreased risk of contamination [ 8 ]. Many thermophilic GHs, such as β- d -glucosidase [ 9 , 10 ], bifunctional cellulolytic enzyme (endo- and exoglucanases) [ 11 ], β- d -xylosidase [ 12 ], and β- d -galactosidase [ 3 , 13 ], have been cloned, heterologously expressed, and biochemically characterized for the purpose of uncovering the catalytic mechanism and evaluating the possibility of industrial applications. Among them, the genus Caldicellulosiruptor has recently attracted high interest for it can produce a diverse set of glycoside hydrolases (GHs) for deconstruction of lignocellulosic biomass [ 7 , 14 , 15 ].…”

Section: Introductionmentioning

confidence: 99%

A multifunctional thermophilic glycoside hydrolase from Caldicellulosiruptor owensensis with potential applications in production of biofuels and biochemicals

Peng

et al. 2016

Biotechnol Biofuels

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BackgroundThermophilic enzymes have attracted much attention for their advantages of high reaction velocity, exceptional thermostability, and decreased risk of contamination. Exploring efficient thermophilic glycoside hydrolases will accelerate the industrialization of biofuels and biochemicals.ResultsA multifunctional glycoside hydrolase (GH) CoGH1A, belonging to GH1 family with high activities of β-d-glucosidase, exoglucanase, β-d-xylosidase, β-d-galactosidase, and transgalactosylation, was cloned and expressed from the extremely thermophilic bacterium Caldicellulosiruptor owensensis. The enzyme exerts excellent thermostability by retaining 100 % activity after 12-h incubation at 75 °C. The catalytic coefficients (kcat/Km) of the enzyme against pNP-β-D-galactopyranoside, pNP-β-D-glucopyranoside, pNP-β-D-cellobioside, pNP-β-D-xylopyranoside, and cellobiose were, respectively, 7450.0, 2467.5, 1085.4, 90.9, and 137.3 mM−1 s−1. When CoGH1A was supplemented at the dosage of 20 Ucellobiose g−1 biomass for hydrolysis of the pretreated corn stover, comparing with the control, the glucose and xylose yields were, respectively, increased 37.9 and 42.1 %, indicating that the enzyme contributed not only for glucose but also for xylose release. The efficiencies of lactose decomposition and synthesis of galactooligosaccharides (GalOS) by CoGH1A were investigated at low (40 g L−1) and high (500 g L−1) initial lactose concentrations. At low lactose concentration, the time for decomposition of 83 % lactose was 10 min, which is much shorter than the reported 2–10 h for reaching such a decomposition rate. At high lactose concentration, after 50-min catalysis, the GalOS concentration reached 221 g L−1 with a productivity of 265.2 g L−1 h−1. This productivity is at least 12-fold higher than those reported in literature.ConclusionsThe multifunctional glycoside hydrolase CoGH1A has high capabilities in saccharification of lignocellulosic biomass, decomposition of lactose, and synthesis of galactooligosaccharides. It is a promising enzyme to be used for bioconversion of carbohydrates in industrial scale. In addition, the results of this study indicate that the extremely thermophilic bacteria are potential resources for screening highly efficient glycoside hydrolases for the production of biofuels and biochemicals.

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A novel thermophilic β-glucosidase from Caldicellulosiruptor bescii: Characterization and its synergistic catalysis with other cellulases

Cited by 23 publications

References 58 publications

Use ofKluyveromyces marxianusprefermented wheat bran as a source of enzyme mixture to improve dough performance and bread biochemical properties

Use ofKluyveromyces marxianusprefermented wheat bran as a source of enzyme mixture to improve dough performance and bread biochemical properties

Functionalized Activated Carbon Derived from Biomass for Photocatalysis Applications Perspective

A multifunctional thermophilic glycoside hydrolase from Caldicellulosiruptor owensensis with potential applications in production of biofuels and biochemicals

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