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Cryptococcus laurentii

This process uses cell suspensions of Cryptococcus laurentii which possess high L-df-amino- -caprolactamase activity, together v/i h Achromobacter oboe cells with high df-amino-df-caprolactam activity. [Pg.143]

Source of Enzyme (s) E. coli B. brevis and Agrobacterium radiobacter B. cereus, Candida bodinii Cryptococcus laurentii and Achromobacter obae P. putid,... [Pg.160]

The first of these enzymes has been studied the most thoroughly. Its activity has been detected in many sources, and purified preparations have been obtained from calf and beef liver,348-349 rat tissues,3498 hen oviduct,350 pea seedlings,351 Cryptococcus laurentii,352 and Aerobacter aerogenes,353 Extensive purification of the liver enzyme was achieved.349... [Pg.364]

Sugita T, Takashima M, Ideka R, Nakase T, Shinoda T Intraspecies diversity of Cryptococcus laurentii as revealed by sequences of internal transcribed spacer regions and 28S rDNA gene and taxonomic positions of C. laurentii clinical isolates. J Clin Microbiol 2000 38 1468-1471. [Pg.295]

Kooiman separated exocellular amylose formed in liquid media at pH < 5 by Cryptococcus albidus and Cryptococcus laurentii var. flavescens NRRL Y-1401 from a polysaccharide containing D-man-nose, D-xylose, and D-glucuronic acid. X-Ray diffraction patterns of the retrograded amyloses were identical with that of tuber starch (B modification). Periodate oxidation, optical rotational measurements, and hypoiodite oxidation data suggested a linear a-D-(l—>4)-linked structure having a chain length of about 44 units for the Cr. albidus amylose. Cryptococcus neoformans produces a crystalline amylose that was isolated by the method of Schoch. It has an iodine value and alpha- and hefa-amylase hydrolysis characteristics similar to those of corn amylose. [Pg.369]

For some years Foray s enzymatic process for L-lysine (L-Lys, 41) was competitive compared with fermentation. This chemoenzymatic L-Lys production was established with a capacity of 5000-10000 t/y. The key intermediate is a-amino-e-caprolactam (ACL), produced from cyclohexanone in a modified Beckmann rearrangement. The enantiospecific hydrolysis forming L-Lys is based on two enzymes L-ACL-hydrolase opens the ring of ACL to L-Lys and in the presence of the ACL-racemase the d-ACL is racemized. Incubating d,l-ACL with cells of Cryptococcus laurentii having l-ACL lactamase activity together with cells of Achromobacter obae with ACL-racemase activity, L-Lys could be obtained in a yield of nearly 100% (Scheme 24) [102]. [Pg.899]

The following organisms were used Cryptococcus laurentii, a yeast Aspergillus fumigatus gp. (Aspergillus fischeri), an enrichment culture isolate and a Fusarium sp. isolated in the laboratory. The fungi were stored as spore suspensions washed from Sabouraud s Dextrose Agar (Difco Detroit, Ml) with 0.1%... [Pg.472]

E1= L-aminolactam-hydrolase, whole cells from Cryptococcus laurentii E2= amino-lactam-racemase, whole cells from Achromobacter obae... [Pg.1443]

L-Lysine, an essential amino acid, is used in very large quantities to supplement human foods and animal feeds. Traditionally, L-Lysine is produced by fermentation processes. An alternative route developed by Toray Ind. involves the chemical synthesis of D/L-a-amino-s-caprolactam followed by the selective hydrolysis of the L-a-amino-s-caprolactam catalyzed by intracellular lactamase in Cryptococcus laurentii, to give L-Lysine. The process can be improved by adding a second micro-organism, Achromobacter obae, containing a-amino-E-caprolactam racemase.Thus, quantitative yields of L-lysine are obtained. [Pg.210]

A nonfermentative yeast. Cryptococcus laurentii, produces a capsular polysaccharide that contains D-mannose, D-xylose, and D-glucuronic acid residues in the approximate molar ratios of 5 2 1. Structural studies indicate that the polysaccharide has a backbone of D-mannose residues, with D-xylose and D-glucuronic acid residues as end groups. A particulate fraction from this organism was shown to catalyze the transfer of the D-xylosyl group from its UDP derivative to acceptor polysaccharides. The transferase can be solubilized with digitonin. Partially de-D-xylosylated capsular polysaccharide from the parent strain is most active as the acceptor, and similarly treated polysaccharides from related species are active to a lesser degree. Neither untreated capsular polysaccharides from these strains nor S. cerevisiae mannan showed any activity as an acceptor. [Pg.409]

Furanocoumarins also have photosensitizing effect on dermatophytes [132]. Xanthotoxin (36) showed activity in darkness against Candida albicans and Cryptococcus laurentii [133]. [Pg.354]

Cell extracts of Cryptococcus laurentii, a yeast which synthesizes amylose when grown at low pH, contain an a-D-glucan phosphorylase (EC 2.4.1.1) which has been characterized. Evidence for a possible role of this enzyme in the biosynthesis of amylose was reported. [Pg.308]

T., Nakase, T. (2003). Three new combinations from the Cryptococcus laurentii complex Cryptococcus aureus, Cryptococcus carnescens and Cryptococcus peneaus. International Journal of Systematic and Evolutionary Microbiology 53,1187-1194. [Pg.173]


See other pages where Cryptococcus laurentii is mentioned: [Pg.188]    [Pg.386]    [Pg.244]    [Pg.366]    [Pg.168]    [Pg.19]    [Pg.20]    [Pg.42]    [Pg.1410]    [Pg.174]    [Pg.275]    [Pg.301]    [Pg.210]    [Pg.262]    [Pg.410]    [Pg.412]    [Pg.416]    [Pg.416]    [Pg.1292]    [Pg.378]    [Pg.15]    [Pg.426]    [Pg.21]    [Pg.136]    [Pg.138]    [Pg.93]    [Pg.93]    [Pg.95]    [Pg.95]    [Pg.150]   
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