{Reference Type}: Journal Article
{Author}: Nanue, Liu; Jing, Zhang; Runguang, Sun; Pingping, Xu; Du Ke; Peijuan, Dou
{Year}: 2011
{Title}: The Effect Mechanism of Ultrasound on the Structure and Biological Activity of Polysaccharide Isolated from Coprinus comatus
{Tag}: 0
{Star}: 0
{Journal}: ACTA CHIMICA SINICA
{Volume}: 69
{Issue}: 15
{Pages}: 1824-1832
{ISBN/ISSN}: 0567-7351
{Keywords}: ASSISTED EXTRACTION; ultrasonic; polysaccharide; monosaccharide composition; structural transformation; GC
{Abstract}: The effect of ultrasonic extraction on the structure and biological activity of polysccharides exert important biological significance and potential value. In this paper, the effect mechanism of ultrasonic extraction on the structure and biological activity of polysccharides was studied. The chemical structures of WCP3a and UCP3a were analyzed by HPLC, GC, GC/MS and their antioxidant activity in vitro were also measured. The results indicated that (1) The WCP3a was composed of mannose, glucose and galactose, but UCP3a was composed of mannose and glucose; (2) WCP3a contained (1 -> 4,6)-linked-alpha-D-mannose, (1 ->)-linked-alpha-D-mannose, (1 -> 3)-linked-alpha-D-glucose, and (1 -> 2,6)-linked-alpha-D-galactose residues, comparing with UCP3a which containing (1 -> 4,6)-linked-alpha-D-mannose, (1 ->)-linked-alpha-D-mannose, (1 -> 3)-linked-alpha-D-glucose, and (1 -> 4)-linked-alpha-D-glucose residues; (3) WCP3a and UCP3a can remove the superoxide anion effectively, and the antioxidant activity of UCP3a in vitro was higher than that of WCP3a; (4) Galactose, the monosaccharide composition of polysaccharide isolated from Coprinus comatus, was transformed to glucose treated by the ultrasound, and the conversion rate first increase and then drop with increasing of ultrasound power and treatment time.
{Author Address}: Shaanxi Normal Univ, Coll Phys & Informat Technol, Lab Biophys & Biomed Engn, Xian 710062, Peoples R China; Shaanxi Normal Univ, Coll Food Engn & Nutr Sci, Xian 710062, Peoples R China; Shaanxi Normal Univ, Coll Phys & Informat Technol, Lab Biophys & Biomed Engn, Xian 710062, Peoples R China; Xian Univ Technol, Fac Sci, Xian 710054, Peoples R China; Shaanxi Normal Univ, Coll Phys & Informat Technol, Lab Biophys & Biomed Engn, Xian 710062, Peoples R China; Shaanxi Normal Univ, Coll Phys & Informat Technol, Lab Biophys & Biomed Engn, Xian 710062, Peoples R China
{Database Provider}: Web of Science SCI
{Language}: Chinese
{Country}: Peoples R China; Peoples R China; Peoples R China

{Reference Type}: Journal Article
{Author}: Ismaya, W. T.; Rozeboom, H. J.; Schurink, M.; Boeriu, C. G.; Wichers, H.; Dijkstra, B. W.
{Year}: 2011
{Title}: Crystallization and preliminary X-ray crystallographic analysis of tyrosinase from the mushroom Agaricus bisporus
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21543865&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Acta Crystallogr Sect F Struct Biol Cryst Commun
{Volume}: 67
{Issue}: Pt 5
{Pages}: 575-8
{DOI}: 10.1107/S174430911100738X
{Date Displayed}: 2011 May 1
{Date}: 2011-05-01
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 21543865
{Keywords}: Agaricus/*enzymology; Crystallization; Crystallography, X-Ray; Enzyme Stability; Monophenol Monooxygenase/*chemistry
{Abstract}: Tyrosinase catalyzes the conversion of tyrosine to dihydroxyphenylalanine quinone, which is the main precursor for the biosynthesis of melanin. The enzyme   from Agaricus bisporus, the common button mushroom, was purified and crystallized in two different space groups. Crystals belonging to space group P2(1) (unit-cell parameters a = 104.2, b = 105.0, c = 119.1 A, beta = 110.6 degrees , four molecules per asymmetric unit) diffracted to 3.0 A resolution. Crystals belonging to space group P2(1)2(1)2 (unit-cell parameters a = 104.0, b = 104.5, c = 108.4 A, two molecules per asymmetric unit) diffracted to 2.6 A resolution. It was essential to include 5 mM HoCl(3) in all crystallization conditions in order to obtain well diffracting crystals.
{Author Address}: Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 7, 9747   AG Groningen, The Netherlands.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Elisashvili, V.; Kachlishvili, E.; Penninckx, M. J.
{Year}: 2008
{Title}: Lignocellulolytic enzymes profile during growth and fruiting of Pleurotus ostreatus on wheat straw and tree leaves
{URL}: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=18595320&query_hl=1
{Tag}: 0
{Star}: 0
{Journal}: Acta Microbiol Immunol Hung
{Volume}: 55
{Issue}: 2
{Pages}: 157-68
{DOI}: 10.1556/AMicr.55.2008.2.7
{Date Displayed}: 2008 Jun
{Date}: 2008-06-01
{Type of Work}: Journal Article; Research Support, Non-U.S. Gov't
{Accession Number}: 18595320
{Keywords}: Fruiting Bodies, Fungal/*growth & development; Fungal Proteins/biosynthesis; Plant Leaves/*microbiology; Plant Stems/*microbiology; Pleurotus/*enzymology/growth & development; Trees/*microbiology; Triticum/*microbiology
{Abstract}: Cultivation of two commercial Pleurotus ostreatus (oyster mushroom) strains was performed in plastic bags. Tree leaves appeared to be an excellent growth substrate for the conversion into fruiting bodies with biological efficiency of 108-118%. The level of enzyme activity was strongly regulated during the life cycle of mushrooms. However, despite the quantitative variations, each strain had a similar pattern of enzyme accumulation in fermentation of both substrates. Laccase and MnP activities were high during substrate colonization and declined rapidly during fruiting body development. On the contrary, in substrate colonization P. ostreatus expressed comparatively low activity of hydrolases. When primordia appeared, the activity of these enzymes sharply increased. Both cellulase and xylanase activity peaked at the mature fruiting body stage. When mushrooms shifted to the vegetative growth, the activity of ligninolytic enzymes   again gradually increased, whereas the activity of hydrolases decreased.
{Author Address}: Durmishidze Institute of Biochemistry and Biotechnology, 0159 Tbilisi, Georgia.
{Language}: eng

{Reference Type}: Journal Article
{Author}: Elisashvili, Vladimir; Kachlishvili, Eva; Penninckx, Michel J.
{Year}: 2008
{Title}: Lignocellulolytic enzymes profile during growth and fruiting of Pleurotus ostreatus on wheat straw and tree leaves
{Tag}: 0
{Star}: 0
{Journal}: ACTA MICROBIOLOGICA ET IMMUNOLOGICA HUNGARICA
{Volume}: 55
{Issue}: 2
{Pages}: 157-168
{ISBN/ISSN}: 1217-8950
{Keywords}: VOLVARIELLA-VOLVACEA; LENTINULA EDODES; CULTIVATION; SUBSTRATE; LACCASE; FERMENTATION; MUSHROOMS; WASTES; FUNGI; Pleurotus ostreatus; lignocellulolytic enzymes; wheat straw; tree leaves
{Abstract}: Cultivation of two commercial Pleurotus ostreatus (oyster mushroom) strains was performed in plastic bags. Tree leaves appeared to be an excellent growth substrate for the conversion into fruiting bodies with biological efficiency of 108-118%. The level of enzyme activity was strongly regulated during the life cycle of mushrooms. However, despite the quantitative variations, each strain had a similar pattern of enzyme accumulation in fermentation of both substrates. Laccase and MnP activities were high during substrate colonization and declined rapidly during fruiting body development. On the contrary, in substrate colonization P. ostreatus expressed comparatively low activity of hydrolases. When primordia appeared, the activity of these enzymes sharply increased. Both cellulase and xylanase activity peaked at the mature fruiting body stage. When mushrooms shifted to the vegetative growth, the activity of ligninolytic enzymes again gradually increased, whereas the activity of hydrolases decreased.
{Author Address}: Durmishidze Inst Biochem & Biotechnol, GE-0159 Tbilisi, Rep of Georgia; Durmishidze Inst Biochem & Biotechnol, GE-0159 Tbilisi, Rep of Georgia; Univ Libre Bruxelles, Lab Physiol & Ecol Microbienne, B-1180 Brussels, Belgium
{Database Provider}: Web of Science SCI
{Language}: English
{Country}: Belgium; Rep of Georgia