Viscosity of β-D-Glucan as a Factor in the Enzymatic Improvement of Barley for Chicks

White, Wayne B.; Bird, H. R.; Sunde, M. L.; Marlett, Judith A.; Prentice, Neville; Burger, W. C.

doi:10.3382/ps.0620853

Cited by 115 publications

(34 citation statements)

References 19 publications

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“…The high amount of (1, 3-1, 4)-␤-glucans present in the endosperm walls is the reason why barley is considered a low-metabolic energy feed grain and therefore is an unacceptable component in chicken feed for poultry. The birds do not produce an enzyme in their gastrointestinal tract to depolymerize the (1, 3-1, 4)-␤-glucans, and this leads to a high viscosity of the feed in the intestine, a limited uptake of nutrients, and sticky droppings adhering to the chickens and the floors of the production cages (36,37). Inclusion of fungal enzyme preparations or purified (1, 3-1, 4)-␤-glucanase from Bacillus amyloliquefaciens to barley diets can overcome the nutritional deficiencies of barley grain and prevent the occurrence of sticky droppings (38,39).…”

Section: Discussionmentioning

confidence: 99%

The production of recombinant proteins in transgenic barley grains

Horvath

Huang

Wong

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

181

113

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Section: Discussionmentioning

confidence: 99%

The production of recombinant proteins in transgenic barley grains

Horvath

Huang

Wong

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

181

113

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“…The enzyme is especially interesting for the brewing industry as P-glucans are the cause of problems in the filtration processes [5], and for broiler chick feedstuffs to improve digestibility [6]. The best characterized P-glucanases are those from genus Bacillus.…”

mentioning

confidence: 99%

Molecular cloning, expression and nucleotide sequence of the endo‐β‐1,3‐1,4‐d‐glucanase gene from Bacillus licheniformis Predictive structural analyses of the encoded polypeptide

Lloberas

Pérez-Pons

Querol

1991

European Journal of Biochemistry

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A Bacillus licheniformis gene coding for an endo-~-l,3-1,4-~-glucanase have been cloned in Escherichia coli and sequenced. The open reading frame contains a sequence of 731 bp, encoding a polypeptide of 243 amino acid residues, with a molecular mass of 27404 Da (24418 Da without the putative signal peptide), which corresponds to the enzyme we had previously isolated and characterized. The signal peptide is functional in E. coli. More than 60% of the endo-P-l,3-1,4-~-glucanase activity is extracellular or periplasmic. The polypeptide is highly similar to other reported Bacillus P-glucanases. Several structural predictive analyses (secondary structure, hydropathic plots, similarity with other related enzymes, etc.) have been performed. From these analyses we assign a tentative three-functional-domain structure for the enzyme (signal peptide, substrate binding and catalytic domains) and a putative lysozyme-like active site.Endo-P-l,3-1,4-~-glucanase is an enzyme that hydrolyzes mixed (1,3-1,4) linkage P-glucans from walls of starchy seed endosperm. /3-glucan is the principal cell wall component of barley endosperm and consists of glucose units joined by 8-1,4 and p-1,3 linkages. Endo-/l-1,3-1,4-~-glucanase hydrolyses 8-1,4 linkages adjacent to /3-1,3, yielding cellobiosyltriose and cellotriosyltetraose [l -31.In a previous paper we have reported the characterization and purification of an endo-fi-l,3-1,4-~-glucanase activity, lichenase, from Bacillu.~ licheniformis [4]. The enzyme is especially interesting for the brewing industry as P-glucans are the cause of problems in the filtration processes [5], and for broiler chick feedstuffs to improve digestibility [6]. The best characterized P-glucanases are those from genus Bacillus. Some genes of this genus, one from Fibrobacter succinogenes and one from barley aleurone, have been cloned and sequenced [7-141. In the present paper we describe the molecular cloning and sequencing of an endo-P-l,3-1,4-~-glucanase gene from B. lichenformis, the secondary structure prediction; hydropathic profile and sequence analyses. From the above, weCorrespondence to

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“…The positive response was assumed to result from amelioration of P-glucan-induced raised viscosity in the small intestine (White et al 1983;Hesselman & Aman 1986;Salih et al 1990) with a corresponding improvement in nutrient utilisation. This premise was supported by the considerable improvement in performance obtained in Trial 1 for meat-chickens given the enzyme supplemented diets based on Fleet barley.…”

Section: Discussionmentioning

confidence: 99%

The effect of feed enzyme supplementation on the performance of meat‐chickens fed enzyme‐responsive barley‐ and wheat/maize‐based diets

King

Moughan

1998

New Zealand Journal of Agricultural Research

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The effect of a commercial feed enzyme complex on the performance of meat-chickens fed barley-and wheat/maize-based pelleted diets was investigated using a variety of barley whose true metabolisable energy (TME) was found to be responsive to enzyme addition and a feed grade wheat and maize. Bioassays for TME of three varieties of barley and of wheat and maize, showed Fleet barley to be responsive to enzyme addition at 100 ppm (P < 0.01) and 200 ppm (P < 0.05). The liveweight, liveweight gain, and feed conversion ratio of meat-chickens receiving Fleet barley-based diets supplemented with an enzyme complex (Roxazyme G) at either 0, 100, or 150 ppm or a wheat/maize-based dietary control with no enzyme inclusion (W/M), was significantly improved by enzyme addition.Enzyme supplementation at 100 and 150 ppm of a W/M-based control diet had no significant effect on the performance of meat-chickens grown to 39 days.Use of feed enzymes may permit greater use of barley in meat-chicken diets and is a strategy capable of conferring performance-enhancing effects in appropriate circumstances. A97041

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Viscosity of β-D-Glucan as a Factor in the Enzymatic Improvement of Barley for Chicks

Cited by 115 publications

References 19 publications

The production of recombinant proteins in transgenic barley grains

The production of recombinant proteins in transgenic barley grains

Molecular cloning, expression and nucleotide sequence of the endo‐β‐1,3‐1,4‐d‐glucanase gene from Bacillus licheniformis Predictive structural analyses of the encoded polypeptide

The effect of feed enzyme supplementation on the performance of meat‐chickens fed enzyme‐responsive barley‐ and wheat/maize‐based diets

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