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Recycling of office waste paper (photocopy, inkjet, and laser prints) is a major problem due to difficulty in removal of nonimpact ink. Biological deinking of office waste paper is reported using several microorganisms and their enzymes. We report here deinking and decolorization of the dislodged ink particles from inkjet printed paper pulp by a marine bacterium, Vibrio alginolyticus isolate no. NIO/DI/32, obtained from marine sediments. Decolorization of this pulp was achieved within 72 h by growing the bacterium in the pulp of 3-6% consistency suspended in seawater. Immobilized bacterial cells in sodium alginate beads were also able to decolorize this pulp within 72 h. The cell-free culture supernatant of the bacterium grown in nutrient broth was not effective in deinking. However, when the culture was grown in nutrient broth supplemented with starch or Tween 80, the cell-free culture supernatant could effectively deink and decolorize inkjet-printed paper pulp within 72 h at 30 degrees C. The culture supernatant of V. alginolyticus grown in the presence of starch or Tween 80 showed 49 U ml(-1) and 33 U ml(-1) amylase and lipase activities, respectively. Dialysis of these culture supernatants through 10 kDa cut-off membrane resulted in a 35-40% reduction in their efficiency in decolorizing the pulp. It appears that amylase and lipase effectively help in dislodging the ink particles from the inkjet printed-paper pulp. We hypothesize that the bacterium might be inducing the formation of low molecular weight free radicals in the culture medium, which might be responsible for decolorization of the pulp.

The ability to degrade organic solid wastes by the fungus Saccobolus saccoboloides was studied. The organism, unusual in such studies, was cultivated in synthetic liquid media with agitation, and on day 8 of growth the mycelium was passed to flasks with trimming. On day 16 of growth, the trimming degradation was assesed by carboxymethylcellulase, xylanase, and amylase activities evaluation, and NaOH 1% hydrolysis. Later on, the type of waste was modified (trimming, filter paper, newspaper, cardboard, sawdust and wood shaving were used) as well as the mass (300-1800 mg/flask). In these cases the enzymatic activities increased between 300 and 600 mg/flask. The total separation of the cellular components in all types of paper and cardboard was observed, together with a high loss of weight. S. saccoboloides was not able to degrade the wood wastes

In order to determine the origin of cellulases in the gut of the earthworm Eisenia fetida andrei, the wall tissues of the different parts of the disinfected gut are cultured in vitro. Enzymatic activities (FPase: filter paper activity; CMCase: carboxymethycellulase, cellobiase) were measured both in the tissues and in the culture medium: the following activities were found, carboxymethycellulase (CMCase), filter paper activity (FPase). The first located in the crop, gizzard and midgut wall, the second in the foregut and midgut wall. The cellobiase was detected only in the crop and gizzard tissues, whereas it is present in each part of the gut of holoxenic worms. This fact indicates that this enzyme is mainly produced by microorganisms ingested. These results allow us to propose the hypothesis of the existence of synergy, for the cellulose hydrolysis between tissular enzymes and cellulolytic microorganisms.

Birch pollen and dog epithelium allergen extracts were studied by ultracentrifugation in linear sucrose gradients. The various sucrose-gradient fractions were then tested for allergenic activity by the paper disc radioallergosorbent test, using sera from allergen sensitive patients.

The use of an amylase-sensitive paper in a screening test for elevated serum amylase levels is described. The paper requires some modification before it can be used as a quantitative amylase assay, but even in its present form it will reliably identify samples with raised amylase levels. In tests with sera received routinely for amylase assay the paper characterised 80% of samples as Normal. Quantitative amylase assay confirmed the results, and thus, even with the present paper, if only the MEDIUM or HIGH sera were sent to the laboratory for full biochemical analysis there would be an 80% decrease in requests.