Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: KEGG:D03434 (Cellulase)
 512 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A new compound endowed with agglutinating activity, designated the flour agglutinin, was extracted from wheat flour with water and purified by gel filtration and ion-exchange chromatography. The haptenic inhibitors of the plant agglutinins do not affect flour agglutinin activity which, on the other hand, is inhibited by D- and L-tryptophan. Flour agglutinin has a molecular weight of about 5 - 10(4) as determined by gel filtration. It consists of a neutral heteropolysaccharide constituted of D-xylose and L-arabinose, and is homogeneous as judged by sedimentation analysis. Flour agglutinin activity is destroyed by treatment with Cellulase 2000 and periodate, but is not affected by alpha-amylase and proteolytic enzymes. Compared to germ agglutinin, flour agglutinin exhibits a peculiar range of cell specificity. It agglutinates several normal cell types, but has no effects on some neoplastic cells tested. Tryptic digestion of erythrocytes does not affect their susceptibility to flour agglutinin-induced agglutination.
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PMID:A new agglutinating activity from wheat flour inhibited by tryptophan. 95 30

Thirty Trichoderma strains representing 15 species within the genus were screened for extracellular production of chitinolytic enzymes in solid substrate fermentation. Trichoderma longibrachiatum IMI 92027 (ATCC 36838) gave the highest yield (5.0 IU/g of dry matter of substrate) after 3 d of fermentation on wheat bran-crude chitin (9:1 mixture) medium. The optimal moisture content (66.7%), chitin content (20%), initial pH of the medium (2.0-5.0), and time course (5 d) of solid substrate fermentation were determined for strain IMI 92027. Cellulase, xylanase, alpha-amylase, and beta-xylosidase activities were also detected. The pH and temperature optima of the chitinase complex of T. longibrachiatum IMI 92027 were 4.5 and 55 degrees C, respectively. The enzyme totally lost its activity at 70 degrees C in 5 min in the absence of the substrate but retained about 15% of its initial activity even at 70 degrees C after a 60-min incubation in the presence of solid substrate fermentation solids. Purification of protein extract from the solid substrate fermentation material revealed high chitinolytic activities between pI 5.9 and 4.8, where N-acetyl-beta-D-hexosaminidase and chitinase peaks have been found in the same pI range. Two chitinases of 43.5 and 30 kDa were purified at acidic pI.
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PMID:Production of chitinolytic enzymes with Trichoderma longibrachiatum IMI 92027 in solid substrate fermentation. 1530 49

Studies were carried out on the enzyme activities of Pleurotus tuber-regium fruitbodies and sclerotia cultivated in various agro-wastes. Higher activities of proteinase, total amylase, and glucose-6-phosphatase were observed in the sporophores compared to the sclerotia. Cellulase, carboxymethylcellulase and lipase values were higher in fruitbodies grown on cotton waste, sawdust of Khaya ivorensis and rice straw (2.4, 0.4 and 3.0 mg/h/mg protein, respectively). Sclerotia propagated on groundnut shells and cocoyam peels had lipase and phenoloxidase levels of 5.8 and 2.6 mg/h/mg protein, respectively. The peroxidase, alpha-amylase and catalase activities were also determined. The implication of these findings in relation to shelf-life, food nutrient, and flavour of this mushroom are discussed.
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PMID:Enzyme activities of Pleurotustuber-regium (Fries) Singer, cultivated on selected agricultural wastes. 1793 60