Bacterial xylanases: biology to biotechnology

Chakdar, Hillol; Kumar, Murugan; Pandiyan, Kurinji; Singh, Arjun; Karthikeyan, N.; Kashyap, Prem Lal; Srivastava, Alok Kumar

doi:10.1007/s13205-016-0457-z

Cited by 162 publications

(132 citation statements)

References 104 publications

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“…From nutritional point of view, bacterial xylanases are advantageous to fungal xylanases as their optimal acting pH are close to that of the intestine, they are thermostable, they have greater aggression towards xylans due to high tenacity of carbohydrate domains, and they are superior to fungal xylanase in degradation of insoluble AX which are the majority of the AX fraction (Courtin et al 2001;Chakdar et al 2016). All these have made xylanases from bacterial origin more amenable to be included in poultry diets.…”

Section: Discussionmentioning

confidence: 99%

Productive performance, nutrient digestibility and intestinal morphometry in broiler chickens fed corn or wheat-based diets supplemented with bacterial- or fungal-originated xylanase

Ghayour-Najafabadi

Khosravinia

Gheisari

et al. 2017

Italian Journal of Animal Science

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An experiment was conducted to evaluate effects of dietary supplementation of a corn-or a wheat-based diet with two sources of exogenous xylanase (fungal or bacterial originated) on productive performance, ileal nutrients digestibility, nitrogen-corrected apparent metabolisable energy (AME n ) and digestive organs morphometry in broiler chickens. Broilers were fed with one of the six dietary treatments consisting of two basal diets (based on corn or wheat) each with or without xylanase (from bacterial or fungal origin) supplementation. Compared with corn-based diet, feeding birds with the wheat-based diet improved weight gain and feed intake by 4.71 and 4.81%, respectively, and ileal digestibility of dry matter and crude protein were greater in birds fed wheat-based diets compared with the birds grown on corn-based during Days 1-21 of age (p<.05). Villus length and villus length to crypt depth ratio increased (p < .05) in birds received wheat-based diets compared with those fed on corn-based diets. Gizzard weight was greater in birds fed with corn-based diets on days 21 and 42 of age by 11.5% and 31.8%, respectively, compared with those received wheat-based diets (p < .05). Supplementing diets with fungal xylanase increased liver weight in birds grown on wheat-based diets compared with those grown on control and corn-based diets, respectively, on Days 21 and 42 of age (p < .05). It was concluded that supplementing a corn-or wheat-based diet with a xylanase of bacterial or fungal origin had no effect on productive performance or AMEn of diets in broiler chickens during the starter and growing periods. ARTICLE HISTORY

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Section: Discussionmentioning

confidence: 99%

Productive performance, nutrient digestibility and intestinal morphometry in broiler chickens fed corn or wheat-based diets supplemented with bacterial- or fungal-originated xylanase

Ghayour-Najafabadi

Khosravinia

Gheisari

et al. 2017

Italian Journal of Animal Science

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“…Of these enzymes, endo-1,4-␤-D-xylanases (EC 3.2.1.8) have been grouped into the glycosyl hydrolase families 5,7,8,10,11,30,43,51,98, and 141 according to the CAZy classification system (4). GH10 and GH11 xylanases are the most common and, while both act on the xylan main chain, these two enzyme types have different folds, substrate specificities, and mechanisms of action (5).…”

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confidence: 99%

Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System

Fredriksen

Stokke

Jensen

et al. 2019

Appl Environ Microbiol

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A two-domain GH10 xylanase-encoding gene (amor_gh10a) was discovered from a metagenomic data set, generated after in situ incubation of a lignocellulosic substrate in hot sediments on the sea floor of the Arctic Mid-Ocean Ridge (AMOR). AMOR_GH10A comprises a signal peptide, a carbohydrate-binding module belonging to a previously uncharacterized family, and a catalytic glycosyl hydrolase (GH10) domain. The enzyme shares the highest sequence identity (42%) with a hypothetical protein from a Verrucomicrobia bacterium, and its GH10 domain shares low identity (24 to 28%) with functionally characterized xylanases. Purified AMOR_GH10A showed thermophilic and halophilic properties and was active toward various xylans. Uniquely, the enzyme showed high activity toward amorphous cellulose, glucomannan, and xyloglucan and was more active toward cellopentaose than toward xylopentaose. Binding assays showed that the N-terminal domain of this broad-specificity GH10 binds strongly to amorphous cellulose, as well as to microcrystalline cellulose, birchwood glucuronoxylan, barley β-glucan, and konjac glucomannan, confirming its classification as a novel CBM (CBM85). IMPORTANCE Hot springs at the sea bottom harbor unique biodiversity and are a promising source of enzymes with interesting properties. We describe the functional characterization of a thermophilic and halophilic multidomain xylanase originating from the Arctic Mid-Ocean Ridge vent system, belonging to the well-studied family 10 of glycosyl hydrolases (GH10). This xylanase, AMOR_GH10A, has a surprisingly wide substrate range and is more active toward cellopentaose than toward xylopentaose. This substrate promiscuity is unique for the GH10 family and could prove useful in industrial applications. Emphasizing the versatility of AMOR_GH10A, its N-terminal domain binds to both xylans and glycans, while not showing significant sequence similarities to any known carbohydrate-binding module (CBM) in the CAZy database. Thus, this N-terminal domain lays the foundation for the new CBM85 family.

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“…Xylanase from bacterial sources are active and stable in a wide range of pH and temperature conditions. Xylanase enzyme exhibited its optimal activity at wide range of incubation conditions, such as temperature from 30 to 60 °C and pH from 5.0 to 9.0 [37]. The present investigation revealed difference between the optimum culture conditions for enzyme production and its activity.…”

Section: Discussionmentioning

confidence: 61%

Production of Industrially Important Enzymes by Thermobacilli Isolated From Hot Springs of India

Dhyani

Gururani

Selim

et al. 2017

RIB

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Enzymes from thermophilic bacteria have received great attention for their potential applications in various industrial sectors. The present study deals with the production of five thermozymes (amylase, lipase, xylanase, protease and cellulase) from 10 thermophilic bacterial species, originally isolated from two hot springs namely Soldhar and Ringigad in Uttarakhand Himalaya, India. The bacterial isolate GBPI_25 produced maximum amylase (1217.86 U/ml) at 45 °C and 5 pH, GBPI 3 produced maximum lipase (22.59 U/ml) at 65 °C and 9 pH, GBPI_25 produced maximum xylanase (98.07 U/ml) at45 °C and 9 pH, GBPI_35 produced maximum protease (16.66 U/ml) at 55 °C and 9 pH, and GBPI 4 produced maximum cellulose (108.68 U/ml) at 45 °C and 5 pH. Crude enzyme preparations showed thermal and pH activities at broad temperature and pH range between 10-100 °C and 3-11 pH, respectively, with different temperature and pH optima. Amylase, xylanase and cellulase showed maximum activity at 50 °C while lipase and protease showed higher activity at 40 and 60 °C, respectively. Enzyme activity at wide temperature range-cellulase and protease from 10-100 °C, amylase and xylanasefrom10-90 °C, and lipase activity from 10-80 °C were the remarkable records from this study. Similarly, pH range for amylase and lipase activity was recorded from 4-11, for xylanase from 3-9, and for protease and cellulase from 3-10. All the thermozymes showed maximum stability at 40 °C and pH 5 except cellulase that showed higher stability at40 °C and neutral pH.

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Bacterial xylanases: biology to biotechnology

Cited by 162 publications

References 104 publications

Productive performance, nutrient digestibility and intestinal morphometry in broiler chickens fed corn or wheat-based diets supplemented with bacterial- or fungal-originated xylanase

Productive performance, nutrient digestibility and intestinal morphometry in broiler chickens fed corn or wheat-based diets supplemented with bacterial- or fungal-originated xylanase

Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System

Production of Industrially Important Enzymes by Thermobacilli Isolated From Hot Springs of India

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