Journal ArticleDOI
Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi.
Purdy Re,Kolattukudy Pe +1 more
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TLDR
The properties of the homogeneous cutinase I, cut inase II, and the nonspecific esterase isolated from the extracellular fluid of cutin-grown Fusarium solani F. pisi were investigated and the two cutinases showed similar substrate concentration dependent, protein concentration dependence, time course profiles, and pH dependence profiles.Abstract:
The properties of the homogeneous cutinase I, cutinase II, and the nonspecific esterase isolated from the extracellular fluid of cutin-grown Fusarium solani F. pisi (R.E. Purdy and P.E. Kolattukudy (1975), Biochemistry, preceding paper in this issue) were investigated. Using tritiated apple cutin as substrate, the two cutinases showed similar substrate concentration dependence, protein concentration dependence, time course profiles, and pH dependence profiles with optimum near 10.0. Using unlabeled cutin, the rate of dihydroxyhexadecanoic acid release from apple fruit cutin by cutinase I was determined to be 4.4 mumol per min per mg. The cutinases hydrolyzed methyl hexadecanoate, cyclohexyl hexadecanoate, and to a much lesser extent hexadecyl hexadecanoate but not 9-hexadecanoyloxyheptadecane, cholesteryl hexadecanoate, or hexadecyl cinnamate. The extent of hydrolysis of these model substrates by cutinase I was at least three times that by cutinase II. The nonspecific esterase hydrolyzed all of the above esters except hexadecyl cinnamate, and did so to a much greater extent than did the cutinases. None of the enzymes hydrolyzed alpha- or beta-glucosides of p-nitrophenol. p-Nitrophenyl esters of fatty acids from C2 through C18 were used as substrates and V's and Kms were determined...read more
Citations
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Journal ArticleDOI
Hydrolysis of butteroil by immobilized lipase using a hollow‐fiber reactor: Part II. Uniresponse kinetic studies
TL;DR: A four‐parameter rate expression is sufficient to model the overall release of free fatty acids from the triglycerides of butterfat as a function of space time and time elapsed after immobilization.
Book ChapterDOI
Lipases or esterases: does it really matter? Toward a new bio-physico-chemical classification.
TL;DR: The present attempt matters scientifically for several reasons: to help newcomers in the field, performing a few key experiments to figure out if a newly isolated esterase is lipolytic or not; to clarify a debate between scientists in theField; and to formulate questions which are relevant to the still unsolved problem of the structure-function relationships of esterases.
Journal ArticleDOI
Targeting microplastic particles in the void of diluted suspensions.
Shohana Islam,Shohana Islam,Lina Apitius,Lina Apitius,Felix Jakob,Felix Jakob,Ulrich Schwaneberg,Ulrich Schwaneberg +7 more
TL;DR: The fusion of the anchor peptide Tachystatin A2 to the bacterial cutinase TCur1278 which accelerated the degradation of polyester-polyurethane nanoparticles by a factor of 6.6 in comparison to wild-type Tcur1278 is reported.
Journal ArticleDOI
Mechanism of action of cutinase: chemical modification of the catalytic triad characteristic for serine hydrolases.
TL;DR: The results of the present chemical modification study indicate that catalysis by cutinase involves the catalytic triad and an acyl-enzyme intermediate, both characteristic for serine proteases.
Journal ArticleDOI
Structural and Functional Studies of a Fusarium Oxysporum Cutinase with Polyethylene Terephthalate Modification Potential.
Maria Dimarogona,Efstratios Nikolaivits,Maria Kanelli,Paul Christakopoulos,Mats Sandgren,Evangelos Topakas +5 more
TL;DR: FoCut5a is the first reported expression and crystal structure determination of a functional cutinase from the mesophilic fungus F. oxysporum with potential application in surface modification of PET synthetic polymers.
References
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Journal ArticleDOI
A simple method for the isolation and purification of total lipides from animal tissues.
TL;DR: In this paper, the authors described a simplified version of the method and reported the results of a study of its application to different tissues, including the efficiency of the washing procedure in terms of the removal from tissue lipides of some non-lipide substances of special biochemical interest.
Journal ArticleDOI
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
Klaus Weber,Mary Osborn +1 more
TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
Journal ArticleDOI
Determination of the structures of cutin monomers by a novel depolymerization procedure and combined gas chromatography and mass spectrometry.
T. J. Walton,P. E. Kolattukudy +1 more
Book ChapterDOI
3 Carboxylic Ester Hydrolases
TL;DR: This chapter focuses on B-esterases, which are inhibited stoichiometrically by organophosphates without hydrolyzing them, which have been formerly known as “ali-esterase” or, because of their wide specificity, as unspecific esterases.
Related Papers (5)
Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isozymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi.
Purdy Re,Kolattukudy Pe +1 more
Determination of the structures of cutin monomers by a novel depolymerization procedure and combined gas chromatography and mass spectrometry.
T. J. Walton,P. E. Kolattukudy +1 more