No abstract

No abstract

Two new sarsolenane diterpenes, dihydrosarsolenone (2), methyl dihydrosarsolenoneate (3), and two new capnosane diterpenes, sarsolilides B (5) and C (6), were isolated together with the known analogue, sarsolilide A (4), from the Hainan soft coral Sarcophyton trocheliophorum Marenzeller. Their structures were elucidated by detailed spectroscopic analysis and by comparison with reported data, leading to a structure revision of sarsolenone (1). The absolute configurations of 2[a] State Key

Lipase production and cell growth of Serratia marcescens ECU1010 were optimized in shake flasks, with lipase production being enhanced 9.5-fold (4,780 U/l) compared with the initial activity (500 U/l). Optimal carbon and nitrogen sources were Tween-80 and peptone, and the optimal ratio of Tween-80 to peptone was 1:3. The optimized cultivation conditions were 25 degrees C and pH 6.5. Lipase activity, particularly specific activity, could be improved by decreasing the cultivation temperature from 35 to 25 degrees C. Enzyme stability was significantly improved by simple immobilization with synthetic adsorption resin no. 8244. After five reaction cycles, enzyme activity decreased only very slightly, while enantioselectivity of the preparation remained constant, and the ees (enantiomeric excess of the remaining substrate) achieved in all cases was higher than 97%. The resin-8244-lipase preparation can be used for efficient enantioselective hydrolysis of trans-3-(4'-methoxyphenyl)glycidic acid methyl ester [(+/-)-MPGM], a key intermediate in the synthesis of Diltiazem.

Marine-polysaccharide degrading enzymes have recently been studied extensively. They are particularly interesting as they catalyze the cleavage of glycosidic bonds in polysaccharide macromolecules and produce oligosaccharides with low degrees of polymerization. Numerous findings have demonstrated that marine polysaccharides and their biotransformed products possess beneficial properties including antitumor, antiviral, anticoagulant, and anti-inflammatory activities, and they have great value in healthcare, cosmetics, the food industry, and agriculture. Exploitation of enzymes that can degrade marine polysaccharides is in the ascendant, and is important for high-value use of marine biomass resources. In this review, we describe research and prospects regarding the classification, biochemical properties, and catalytic mechanisms of the main types of marine-polysaccharide degrading enzymes, focusing on chitinase, chitosanase, alginate lyase, agarase, and carrageenase, and their product oligosaccharides. The state-of-the-art discussion of marine-polysaccharide degrading enzymes and their properties offers information that might enable more efficient production of marine oligosaccharides. We also highlight current problems in the field of marine-polysaccharide degrading enzymes and trends in their development. Understanding the properties, catalytic mechanisms, and modification of known enzymes will aid the identification of novel enzymes to degrade marine polysaccharides and facilitation of their use in various biotechnological processes. K E Y W O R D S agarase, alginate lyase, carrageenase, chitinase, chitosanase 1 INTRODUCTION Ocean occupies >70% of the global surface, and the vast oceanic water environment has spawned large and complex marine ecosystems with rich biodiversity. There is a wide variety of marine resources, however, they are largely unexploited. This situation makes the marine environment very attractive for bioprospecting to discover new functions and molecules (Arnaud-Haond, Arrieta, & Duarte, 2011). Research into marine compounds, especially polysaccharides from renewable biomass, is attracting increasing attention. Polysaccharides make up one of the largest

No abstract

No abstract

[structure: see text] The preparation of three new chiral thiazines from ribose is described. Two of these are dihydroxytetrahydro-1H-pyrrolo[2,1-c][1,4]benzothiazines with iminopentitol substructures corresponding to the L-lyxo and D-ribo configurations. They were designed to present a favorable transition-state mimic for the inhibition of ribosidases. This new thiazine class opens the way to the development of new inhibitors to carbohydrate processing enzymes of therapeutic importance such as nucleoside hydrolases and purine nucleoside phosphorylases.