Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley

Manners, D. J.; Wilson, Glynn

doi:10.1016/s0008-6215(00)87061-5

Cited by 36 publications

(17 citation statements)

References 34 publications

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“…Cellobiase activity fell by approximately one third during kilning (Figures 3c, d), the severity of the kilning process affecting the degree of loss. [24][25][26][27][28][29][30][31][32][33][34] Effect ofgibberellic acid on individual malt enzymes A preliminary examination of gibbcrellic acid (GA3) stimulated malt extract indicated an increase in endo-1,3; 1,4-P-glucanase activity of 5-fold and in endo-l,3-Pglucanase activity of 3-fold (Table I, Figure 3e). By specific activity, however, the corresponding changes were an increase of 30% and a decrease of 20% respectively (Table 1).…”

Section: Development Ofp-glucanases In Germinating Barleymentioning

confidence: 99%

“…27 In contrast, the endo-1,3-P-D-glucanase (E.C.3.2.1.39) and endo-1.3;l,4-P-D-glucanasc (E.C.3.2.1.73) activities were concluded to be constitutive to the germinating barley grain. [24][25][26][27][28][29][30][31][32][33][34][35][36][37][38] Endo-1,3-P-glucanase has been isolated from both germi nated and kilned barley malt by several investigators. i23>28…”

Section: Introductionmentioning

confidence: 99%

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The DEVELOPMENT OF Β-D-Glucanases DURING THE GERMINATION OF BARLEY AND THE EFFECT OF KILNING ON INDIVIDUAL ISOENZYMES†

Brunswick

Manners

Stark

1987

Journal of the Institute of Brewing

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Two endo-1,3;1,4-p-D-glucanase isoenzymes developed in response to gibberellic acid, during the germination of barley. Two endo-1,3-p-D-glucanases, one present in ungerminated, steeped grain, also developed but did not appear to be markedly stimulated by the hormone. A comparison of crude and partially purified malt extracts highlighted the errors that are involved in the specific determination of endo-1,3;1,4-p-glucanase activity in crude extracts. The development and effect of kilning on individual malt isoenzymes was demonstrated by carboxymethylcellulose (CM-cellulose) chromatography profiles.Kilning and dry-milling of germinated barley caused losses of 80-90% in the specific endo-1,3;1,4-p-glucanase activity. The effect was less pronounced if wet-milling was substituted for dry-milling. Extraction studies and CM-cellulose chromatography profiles indicated that both endo-1,3:1,4-pglucanase isoenzymes were heat labile and were particularly susceptible to oxidation. In contrast, endo-1,3-p-glucanase activity and cellobiase activity in malt extracts were less affected by the kilning process or extraction procedures. Preliminary results suggested that one of the endo-1,3-p-glucanase isoenzymes was more sensitive to kilning.

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Section: Development Ofp-glucanases In Germinating Barleymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The DEVELOPMENT OF Β-D-Glucanases DURING THE GERMINATION OF BARLEY AND THE EFFECT OF KILNING ON INDIVIDUAL ISOENZYMES†

Brunswick

Manners

Stark

1987

Journal of the Institute of Brewing

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“…Although the barley endo-l,3-~-glucanase has long been recognized as a separate enzyme from the endo-1,3;1,4-13-glucanase (6,16), its function in the kernel is still not fully understood. The enzyme is specific for 1,3-13-glucans and will not degrade the mixed-linkage 13-glucan to oligosaccharides (20). It thus belongs to the enzyme category EC 3.2.1.39 as opposed to EC 3.2.1.6.…”

Section: Introductionmentioning

confidence: 99%

Purification and amino acid sequence determination of an endo-1,3-β-glucanase from barley

Ballance

Svendsen

1988

Carlsberg Res. Commun.

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An endo-l,3-[3-glucanase was purified from malted barley by ion exchange column chromatography. The purified enzyme protein was demonstrated to be free of other proteins by SDS-polyacrylamide gel electrophoresis and had a molecular weight of 32,000. The amino acid composition of the protein was determined and the complete amino acid sequence was constructed from overlapping peptides generated by enzymatic as well as chemical cleavages. The molecule contains 306 amino acids arranged in one peptide chain. The molecular weight calculated from the sequence is 32,286. The sequence of the 1,3-[3-glucanase shows approximately 50% positional identity with two other I~-glucanases from barley and tobacco, respectively.

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“…*' The bulk of the pi,4 glucanase associated with malt arises from microbes associated with the husk, so that this enzyme is unlikely to be a major contributor to cytolysis. [17][18][19][20][21][22] Recently, Woodward & Fincher made a detailed study of two p-glucanascs from malted barley which arc specific to mixed-linkage p-glucans.2<)-JI However, in common with most other studies of this particular category of glucanases, a gum* preparation from denatured barley was used as the substrate to assay the enzyme. Bathgate and co-workers showed that gum differs from solubilised hemicellulosc in several respects, including its different susceptibility to pi, 3-glucanase,"12 and it was concluded that once it is solubil ised by enzyme, the hemicellulosic P-glucan is degraded by endo-P1,3-glucanase to give smaller glucans which are sus ceptible to the action of the endo-barley-P-glucanase."…”

Section: Introductionmentioning

confidence: 99%

The DEGRADATION OF Β-Glucan DURING MALTING AND MASHING: THE ROLE OF Β-Glucanase

Bamforth¹,

Martin²

1983

Journal of the Institute of Brewing

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Significant p -glucanolysis takes place during mashing and is catalysed by a P -glucanase which is specific to mixed-linkage p-glucans. The enzyme develops during the germination of barley, but is rapidly and extensively destroyed in kilning. Partially-purified preparations of B-glucanase are protected from denaturation by heat if their solutions are adjusted to pH 4 or if bovine serum albumin is added. However the most effective stabiliser of the enzyme is reduced glutathione. Oligosaccharides containing three and four glucosyl units are produced by the action of p-glucanase and they are further converted during malting and mashing by a different enzyme(s) to disaccharides and glucose.

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Purification and properties of an endo-(1→3)-β-d-glucanase from malted barley

Cited by 36 publications

References 34 publications

The DEVELOPMENT OF Β-D-Glucanases DURING THE GERMINATION OF BARLEY AND THE EFFECT OF KILNING ON INDIVIDUAL ISOENZYMES†

The DEVELOPMENT OF Β-D-Glucanases DURING THE GERMINATION OF BARLEY AND THE EFFECT OF KILNING ON INDIVIDUAL ISOENZYMES†

Purification and amino acid sequence determination of an endo-1,3-β-glucanase from barley

The DEGRADATION OF Β-Glucan DURING MALTING AND MASHING: THE ROLE OF Β-Glucanase

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