Enzymatic synthesis of arbutin undecylenic acid ester and its inhibitory effect on mushroom tyrosinase

2006 ◽  
Vol 29 (3) ◽  
pp. 481-486 ◽  
Author(s):  
Y. Tokiwa ◽  
M. Kitagawa ◽  
T. Raku
Keyword(s):  
Enzymatic Synthesis ◽  
Acid Ester ◽  
Inhibitory Effect ◽  
Undecylenic Acid ◽  
Mushroom Tyrosinase

Enzymatic synthesis of arbutin undecylenic acid ester and its inhibitory effect on melanin synthesis

2007 ◽  
Vol 17 (11) ◽  
pp. 3105-3108 ◽  
Author(s):  
Yutaka Tokiwa ◽  
Masaru Kitagawa ◽  
Takao Raku ◽  
Shusaku Yanagitani ◽  
Kenji Yoshino
Keyword(s):  
Enzymatic Synthesis ◽  
Acid Ester ◽  
Inhibitory Effect ◽  
Undecylenic Acid ◽  
Melanin Synthesis

Green Enzymatic Synthesis of L-Ascorbyl Fatty Acid Ester: An Antioxidant

2009 ◽  
Vol 39 (7) ◽  
pp. 1143-1151 ◽  
Author(s):  
Mazaahir Kidwai ◽  
Poonam Mothsra ◽  
Namita Gupta ◽  
S. Suresh Kumar ◽  
Rani Gupta
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Ester ◽  
Enzymatic Synthesis ◽  
Acid Ester

Enzymatic synthesis of amino acid ester of butyl α-D-glucopyranoside

1994 ◽  
Vol 35 (21) ◽  
pp. 3535-3536 ◽  
Author(s):  
Jean Fabre ◽  
François Paul ◽  
Pierre Monsan ◽  
Casimir Blonski ◽  
Jacques Périé
Keyword(s):  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Acid Ester ◽  
Amino Acid Ester

scholarly journals An Inhibitory Effect for Putrefaction of Boiled Milled Rice by Formulation Containing Glycerin Fatty Acid Ester

1975 ◽  
Vol 28 (5) ◽  
pp. 263-269
Author(s):  
Zenichi MORI ◽  
Kazunori NISHIZAWA ◽  
Mamoru KATSUMI
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Ester ◽  
Acid Ester ◽  
Inhibitory Effect ◽  
Milled Rice

scholarly journals The role of alkyl chain length in the inhibitory effect n-alkyl xanthates on mushroom tyrosinase activities.

2007 ◽  
Vol 54 (1) ◽  
pp. 183-191 ◽  
Author(s):  
Ali Akbar Saboury ◽  
Mahdi Alijanianzadeh ◽  
Hasan Mansoori-Torshizi
Keyword(s):  
Competitive Inhibition ◽  
Inhibitory Effect ◽  
Uv Spectrophotometry ◽  
Negative Cooperativity ◽  
Mushroom Tyrosinase ◽  
Uncompetitive Inhibition ◽  
Sodium Phosphate Buffer ◽  
Catecholase Activity ◽  
Hydrophobic Tail

Sodium salts of four n-alkyl xanthate compounds, C2H5OCS2Na (I), C3H7OCS2Na (II), C4H9OCS2Na (III), and C6H13OCS2Na (IV) were synthesized and examined for inhibition of both cresolase and catecholase activities of mushroom tyrosinase (MT) in 10 mM sodium phosphate buffer, pH 6.8, at 293 K using UV spectrophotometry. 4-[(4-Methylbenzo)azo]-1,2-benzendiol (MeBACat) and 4-[(4-methylphenyl)azo]-phenol (MePAPh) were used as synthetic substrates for the enzyme for catecholase and cresolase reactions, respectively. Lineweaver-Burk plots showed different patterns of mixed, competitive or uncompetitive inhibition for the four xanthates. For the cresolase activity, I and II showed uncompetitive inhibition but III and IV showed competitive inhibition pattern. For the catecholase activity, I and II showed mixed inhibition but III and IV showed competitive inhibition. The synthesized compounds can be classified as potent inhibitors of MT due to their Ki values of 13.8, 11, 8 and 5 microM for the cresolase activity, and 1.4, 5, 13 and 25 microM for the catecholase activity for I, II, III and IV, respectively. For the catecholase activity both substrate and inhibitor can be bound to the enzyme with negative cooperativity between the binding sites (alpha > 1) and this negative cooperativity increases with increasing length of the aliphatic tail of these compounds. The length of the hydrophobic tail of the xanthates has a stronger effect on the Ki values for catecholase inhibition than for cresolase inhibition. Increasing the length of the hydrophobic tail leads to a decrease of the Ki values for cresolase inhibition and an increase of the Ki values for catecholase inhibition.

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