Results 351 to 360 of about 297,801 (378)

Enhancement of the antioxidant and starch hydrolase inhibitory activities of king coconut water (Cocos nucifera var. aurantiaca) by fermentation with kombucha 'tea fungus'.

, 2016
Summary Enhancement of antioxidant and starch hydrolase inhibitory properties of king coconut water when subjected to fermentation with the ‘tea fungus’ was evaluated.
Mindani I. Watawana, Nilakshi Jayawardena, Chaminie B. Gunawardhana, V. Waisundara   +3 more
semanticscholar   +1 more source

Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Partial amino acid sequence of 80 kDa oxidized protein hydrolase (OPH), a serine protease present in human erythrocyte cytosol (Fujino et al., J. Biochem. 124 (1998) 1077-1085) that is adherent to oxidized erythrocyte membranes and preferentially degrades oxidatively damaged proteins (Beppu et al., Biochim. Biophys. Acta 1196 (1994) 81-87; Fujino et al.
Hideyo Yasuda, Kazuomi Watanabe, Kiyomi Kikugawa, Masatoshi Beppu, Tomofumi Fujino   +4 more
openaire   +3 more sources

Endo-Xylogalacturonan Hydrolase

2003
Commercial pectinases used in apple juice manufacturing contain a mixture of pectin-degrading enzyme activities. Nevertheless, fragments of branched pectic molecules (or pectic hairy regions) are resistant to degradation, and can cause membrane fouling in the final ultrafiltration step of concentrated apple juice.
P.J.A. Meeuwsen, C. J. B. van der Vlugt-Bergmans, Jean-Paul Vincken, Margareta Adriana Herweijer, Gerrit Beldman, Alphons G. J. Voragen, A.J.J. van Ooyen, A.J.J. van Ooyen   +7 more
openaire   +3 more sources

The Telltale Structures of Epoxide Hydrolases

Drug Metabolism Reviews, 2003
Traditionally, epoxide hydrolases (EH) have been regarded as xenobiotic-metabolizing enzymes implicated in the detoxification of foreign compounds. They are known to play a key role in the control of potentially genotoxic epoxides that arise during metabolism of many lipophilic compounds.
Arand, Michael, Cronin, Annette, Oesch, Franz, Mowbray, Sherry L, Jones, T Alwyn   +4 more
openaire   +3 more sources

Hydrolase-catalyzed asymmetric carbon–carbon bond formation in organic synthesis

, 2015
Enzyme catalytic promiscuity, in which the active site of an enzyme has the ability to catalyze more than one chemical transformation, has received widespread attention as more catalytic promiscuities of existing enzymes have been discovered.
Zhi Guan, Ling-Yu Li, Yan‐Hong He
semanticscholar   +1 more source

Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family.

Biochemistry, 2010
Currently, the relatively high cost of enzymes such as glycoside hydrolases that catalyze cellulose hydrolysis represents a barrier to commercialization of a biorefinery capable of producing renewable transportable fuels such as ethanol from abundant ...
P. Harris, D. Welner, K. Mcfarland, E. Re, J. Poulsen, K. Brown, R. Salbo, H. Ding, E. Vlasenko, Sandy Merino, Feng Xu, J. Cherry, S. Larsen, L. Leggio   +13 more
semanticscholar   +1 more source

The Nudix hydrolase superfamily

Cellular and Molecular Life Sciences CMLS, 2005
Nudix hydrolases are found in all classes of organism and hydrolyse a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity.
openaire   +3 more sources

S-Adenosylhomocysteine Hydrolase

1986
S-Adenosylhomocysteine hydrolase (AdoHcyase; EC 3.3.1.1) catalyzes the overall reaction first described by de la Haba and Cantoni (1957):
Peter K. Chiang, George A. Miura
openaire   +2 more sources

Dimetallic hydrolases and their models

Current Opinion in Chemical Biology, 2000
Recent mechanistic studies of Fe3+/M2+ purple acid phosphatase present conflicting pictures about the roles of the metals. Recent model studies with Co3+/Co3+ and Fe3+/Fe3+ complexes have supported each conflicting mechanism for phosphate hydrolysis.
openaire   +3 more sources

Thermal resistance of pantetheine hydrolase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
Pantetheine hydrolase from pig kidney shows a very high resistance to denaturation with chemical denaturants, being unfolded at concentrations of guanidinium chloride higher than 6.5 M. On the contrary, chemical inactivation, followed by recording catalytic activity, occurs before conformational changes can be detected by fluorimetric or spectroscopic ...
PITARI, Giuseppina, Antonini G, Mancini R, Dupre S.   +3 more
openaire   +2 more sources