Improvement of the quality of wheat bread by addition of glycoside hydrolase family 10 xylanases. Appl Microbiol Biotechnol
Although many xylanases are widely used in the baking industry, only one glycoside hydrolase family 10 (GH 10) xylanase has previously been reported to be effective in baking. In this study, we compared the effectiveness of two GH 10 xylanases, psychrophilic XynA from Glaciecola mesophila and mesophilic EX1 from Trichoderma pseudokoningii, in bread making. The optimal dosages needed to improve wheat flour dough and bread quality were 270-U/kg flour for EX1 and 0.9-U/kg flour for XynA. At their optimal dosage, both XynA and EX1 had significant dough-softening ability, resulting in a 50% reduction in Brabender units. XynA was more effective than EX1 in reducing the time to reach maximum consistency. XynA and EX1 showed similar effects in improving the bread volume (~30% increase). EX1 was more effective in reducing the initial crumb firmness. Although both enzymes exhibited similar anti-staling effects on the bread, based on a decrease in the bread firmness, XynA had a greater effect on reducing the firming rate, and EX1 showed an enhanced reduction in the initial firmness. These results show that these two GH 10 xylanases have unique advantages in improving dough and bread quality and indicate their potential in bread making.
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mesophila KMM241 was isolated from a specimen of marine invertebrate Halocynthia aurantium . In our previous studies, a cold-adapted and salt-tolerant GH family 10 endo-β-1,4-xylanase (XynA) from G.
mesophila KMM241 was expressed and characterized , and the effect of XynA on bread baking was studied . In this study, another xylanase, XynB, from G. mesophila KMM241 was expressed and characterized, which showed that XynB was a GH family 8 xylanase containing an N-terminal domain and a catalytic domain. "
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ABSTRACT: Marine xylanases are rather less studied compared to terrestrial xylanases. In this study, a new xylanase gene, xynB, was cloned from the marine bacterium, Glaciecola mesophila KMM241, and expressed in Escherichia coli. xynB encodes a multi-domain xylanase XynB of glycoside hydrolase (GH) family 8. The recombinant XynB comprises an N-terminal domain (NTD) with unknown function and a catalytic domain, which is structurally novel among the characterized xylanases of GH family 8. XynB has the highest identity (38%) to rXyn8 among the characterized xylanases. The recombinant XynB showed maximal activity at pH 6-7 and 35 °C. It is thermolabile and salt-tolerant. XynB is an endo-xylanase that demands at least five sugar moieties for effective cleavage and to hydrolyze xylohexaose and xylopentaose into xylotetraose, xylotriose and xylobiose. NTD was expressed in Escherichia coli to analyze its function. The recombinant NTD exhibited a high binding ability to insoluble xylan and avicel and little binding ability to chitosan and chitin. Since the NTD shows no obvious homology to any known carbohydrate-binding module (CBM) sequence in public databases, XynB may contain a new type of CBM.
Marine Drugs 04/2013; 11(4):1173-87. DOI:10.3390/md11041173 · 2.85 Impact Factor
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ABSTRACT: The bread-improving potential of three psychrophilic xylanases from Pseudoalteromonas haloplanktis TAH3A (XPH), Flavobacterium sp. MSY-2 (rXFH), and unknown bacterial origin (rXyn8) was compared to that of the mesophilic xylanases from Bacillus subtilis (XBS) and Aspergillus aculeatus (XAA). XPH, rXFH, and rXyn8 increased specific bread volumes up to 28%, 18%, and 18%, respectively, while XBS and XAA gave increases of 23% and 12%, respectively. This could be related to their substrate hydrolysis behavior. Xylanases with a high capacity to solubilize water-unextractable arabinoxylan (WU-AX) during mixing, such as XBS and XPH, increased bread volume more than xylanases that mainly solubilized WU-AX during fermentation, such as rXFH, rXyn8, and XAA. Irrespective of their intrinsic bread-improving potential, the dosages needed to increase bread volume to a similar extent were much lower for psychrophilic than for mesophilic xylanases. The xylanase efficiency mainly depended on the enzyme's temperature activity profile and its inhibition sensitivity.
Journal of Agricultural and Food Chemistry 08/2011; 59(17):9553-62. DOI:10.1021/jf201752g · 2.91 Impact Factor
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ABSTRACT: Four different grain cell wall staining techniques were compared. Two techniques specifically detected arabinoxylan (AX). The first technique used a xylanase probe, while the other one was based on immunolabeling of AX using monoclonal antibodies. The two other staining techniques, one based on Calcofluor and the other on immunolabeling using monoclonal antibodies, stained mixed-linkage fl-glucan. Cell walls of wheat, barley, oat and rye grains, differing both in content and location of AX and fl-glucan, were examined. The staining methods were complementary to each other in revealing the location and distribution of the major cereal dietary fiber components AX and fl-glucan in the different grains. AX was mostly concentrated in nucellar epidermis and aleurone cells, whereas fl-glucan was concentrated more in subaleurone cells. Furthermore, in the case of barley and rye, the endosperm cell walls also contained high amounts of beta-glucan. Interestingly, beta-glucan in rye and barley endosperm cell walls was located adjacent to the cell contents, suggesting that it is not evenly distributed in the endosperm cell walls. The results give new insight into the structure of the cereal dietary fiber complex. Further development of microscopic techniques will help in elucidating the cereal cell wall structure even in more detail.
Journal of Cereal Science 11/2011; 54(3):363. DOI:10.1016/j.jcs.2011.07.003 · 2.09 Impact Factor
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