Literature DB >> 947540

Purification of malted-barley endo-beta-D-glucanases by ion-exchange chromatography: some properties of an endo-barley-beta-D-glucanase.

D J Manners, G Wilson.   

Abstract

Two endo-beta-D-glucanases which act, respectively, on (1 leads to 3)-beta-D-glucans and barley beta-D-glucan have been isolated from malted barley, and purified by ion-exchange chromatography. The latter enzyme is highly specific for barley beta-D-glucan, and has no action on either (1 leads to 3)- or (1 leads to 4)-beta-D-glucans. It will also act on dyed barley-beta-D-glucan. Certain group-specific reagents inhibit the endo-barley-beta-D-glucanase and the endo-(1 leads to 3)-beta-D-glucanase to similar extents.

Entities:  

Mesh:

Substances:

Year:  1976        PMID: 947540     DOI: 10.1016/s0008-6215(00)83221-8

Source DB:  PubMed          Journal:  Carbohydr Res        ISSN: 0008-6215            Impact factor:   2.104


  3 in total

1.  Preparation and Properties of a beta-d-Glucanase for the Specific Hydrolysis of beta-d-Glucans.

Authors:  D J Huber; D J Nevins
Journal:  Plant Physiol       Date:  1977-08       Impact factor: 8.340

2.  beta-d-Glucan Hydrolase Activity in Zea Coleoptile Cell Walls.

Authors:  D J Huber; D J Nevins
Journal:  Plant Physiol       Date:  1980-05       Impact factor: 8.340

3.  Partial purification of endo- and exo-β-D-glucanase enzymes from Zea mays L. seedlings and their involvement in cell-wall autohydrolysis.

Authors:  D J Huber; D J Nevins
Journal:  Planta       Date:  1981-03       Impact factor: 4.116

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.