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		题名	作者	年代	出处	被引量
	1	Structure of Pseudorandom Numbers Derived from Fermat Quotients 显示文摘	CHEN Zhixiong OSTAFE A WINTERHOF A	2010	Lecture Notes in Computer Science2010，，：	1
	2	Pseudorandomness and dy namics of Fermat quotients显示文摘	Ostafe A Shparlinski I E	2011	SIAM J Discr Math2011，25，1：	1
	3	Pseudorandomness and Dy- namics of Fermat Quotients 显示文摘	OSTAFE A SHPARLINSKI I E	2011	SIAM Journal on Discrete Mathematics2011，25，1：	1
	4	A high-throughput eellulase screening system based on droplet mierofluidies显示文摘	Ostafe R Prodanovic R Ung W L	2014	Biomierofluidies2014，8，4：	1
	5	Multivariate permutation polynomial systems and nonlinear pseudorandom number generators显示文摘	Ostafe A		0，，03：	1
	6	Nonlinear correlations in the hydrophobicity and average flexibility along the glycolytic enzymes sequences显示文摘	Alecu Ciorsac Dana Craciun Vasile Ostafe Adriana Isvoran	2011	Chaos, Solitons and Fractals2011，，4：	1
	7	Preparation, modification, and applications of chitin nanowhiskers: a review显示文摘	Mincea M Negrulescu A Ostafe V	2012	Reviews on Advanced Materials Science2012，30，3：	1
	8	Improved degradation of azo dyes by lignin peroxidase following mutagenesis at two sites near the catalytic pocket and the application of peroxidase-coated yeast cell walls显示文摘The enzymatic degradation of azo dyes is a promising alternative to ineffective chemical and physical remediation methods.Lignin peroxidase(LiP)from Phanerochaete chrysosporium is a hemecontaining lignin-degrading oxidoreductase that catalyzes the peroxide-dependent oxidation of diverse molecules,including industrial dyes.This enzyme is therefore ideal as a starting point for protein engineering.Accordingly,we subjected two positions(165 and 264)in the environment of the catalytic Trp171 residue to saturation mutagenesis,and the resulting library of 104 independent clones was expressed on the surface of yeast cells.This yeast display library was used for the selection of variants with the ability to break down structurally-distinct azo dyes more efficiently.We identified mutants with up to 10-fold greater affinity than wild-type LiP for three diverse azo dyes(Evans blue,amido black 10B and Guinea green)and up to 13-fold higher catalytic activity.Additionally,cell wall fragments displaying mutant LiP enzymes were prepared by toluene-induced cell lysis,achieving significant increases in both enzyme activity and stability compared to a whole-cell biocatalyst.LiPcoated cell wall fragments retained their initial dye degradation activity after 10 reaction cycles each lasting 8 h.The best-performing mutants removed up to 2.5-fold more of each dye than the wild-type LiP in multiple reaction cycles.	Karla IlićĐurđić Raluca Ostafe Olivera Prodanović AleksandraĐurđevićĐelmaš Nikolina Popović Rainer Fischer Stefan Schillberg Radivoje Prodanović	2021	Frontiers of Environmental Science & Engineering2021，15，2：	1

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