ENZYMATIC DEGRADATION OF THE CHOLESTEROL SIDE CHAIN IN CELL-FREE PREPARATIONS

1953 ◽  
Vol 75 (6) ◽  
pp. 1511-1512 ◽  
Author(s):  
Christian B. Anfinsen ◽  
Marjorie G. Horning
1975 ◽  
Vol 53 (1) ◽  
pp. 37-41 ◽  
Author(s):  
Brian G. Brownlee ◽  
Ross H. Hall ◽  
C. Dennis Whitty

An enzyme preparation from immature corn kernels catalyzes cleavage of N6-(Δ2-isopentenyl) adenine to give the aldehyde, 3-methyl-2-butenal, as the major side-chain derived product. This product, in the form of the semicarbazone, was identical with an authentic product by several criteria: chromatographic behavior, mass and ultraviolet spectra.


Materials ◽  
2021 ◽  
Vol 14 (3) ◽  
pp. 503
Author(s):  
Liyuan Hou ◽  
Erica L.-W. Majumder

Polystyrene (PS) is one of the main polymer types of plastic wastes and is known to be resistant to biodegradation, resulting in PS waste persistence in the environment. Although previous studies have reported that some microorganisms can degrade PS, enzymes and mechanisms of microorganism PS biodegradation are still unknown. In this study, we summarized microbial species that have been identified to degrade PS. By screening the available genome information of microorganisms that have been reported to degrade PS for enzymes with functional potential to depolymerize PS, we predicted target PS-degrading enzymes. We found that cytochrome P4500s, alkane hydroxylases and monooxygenases ranked as the top potential enzyme classes that can degrade PS since they can break C–C bonds. Ring-hydroxylating dioxygenases may be able to break the side-chain of PS and oxidize the aromatic ring compounds generated from the decomposition of PS. These target enzymes were distributed in Proteobacteria, Actinobacteria, Bacteroidetes, and Firmicutes, suggesting a broad potential for PS biodegradation in various earth environments and microbiomes. Our results provide insight into the enzymatic degradation of PS and suggestions for realizing the biodegradation of this recalcitrant plastic.


1999 ◽  
Vol 65 (6) ◽  
pp. 2446-2452 ◽  
Author(s):  
Harald J. Ruijssenaars ◽  
Jan A. M. de Bont ◽  
Sybe Hartmans

ABSTRACT The xanthan-degrading bacterium Paenibacillus alginolyticus XL-1, isolated from soil, degrades approximately 28% of the xanthan molecule and appears to leave the backbone intact. Several xanthan-degrading enzymes were excreted during growth on xanthan, including xanthan lyase. Xanthan lyase production was induced by xanthan and inhibited by glucose and low-molecular-weight enzymatic degradation products from xanthan. A xanthan lyase with a molecular mass of 85 kDa and a pI of 7.9 was purified and characterized. The enzyme is specific for pyruvated mannosyl side chain residues and optimally active at pH 6.0 and 55°C.


1995 ◽  
Vol 41 (13) ◽  
pp. 138-142 ◽  
Author(s):  
R. H. Marchessault ◽  
F. G. Morin ◽  
S. Wong ◽  
I. Saracovan

In vitro preparation of long side chain poly(3-hydroxyalkanoate) artificial granule suspensions that mimic the "as biosynthesized" inclusions in vivo is reported. Elastomeric poly(3-hydroxyalkanoate) can be made into an aqueous suspension of noncrystalline, submicron-sized particles. Light-scattering measurements on these suspensions showed polymer particles in the range of 90–200 nm in diameter. High-resolution 13C-NMR studies demonstrated the noncrystalline character of the in vitro artificial granules. Upon drying at room temperature, the suspensions yielded a continuous film resulting from the coalescence of these polymers with a low glass transition temperature and low Young's modulus. Aqueous suspensions of poly(3-hydroxyoctanoate) are ideal substrates for enzymatic degradation studies because of their stability and purity, since they are self-stabilized. The range of poly(3-hydroxyalkanoates) that can be converted to artificial granules and the methods of preparation are described.Key words: poly(3-hydroxyalkanoate), artificial granules, in vitro bacterial inclusions, enzyme model substrates, poly(3-hydroxyoctanoate).


2009 ◽  
Vol 6 (5) ◽  
pp. 754-763 ◽  
Author(s):  
Kun Li ◽  
Na Wang ◽  
Fan Yang ◽  
Zhong-Wei Zhang ◽  
Li-Hong Zhou ◽  
...  

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