Effect of short‐term anaerobic conditions on the production of volatiles,activity of alcohol acetyltransferase and other quality traits of ripened bananas. Sumithra K Wendakoon. Yoshinori Ueda. Yoshihiro Imahori. Megumi Ishimaru. Journal of the Science of Food and Agriculture, 2006; 86: 1475–1480

The original article to which this Erratum refers was published in Journal of the Science of Food and Agriculture, 2006; 86: 1475–1480.     

Estimation of daily intake of phenols in hospital meal samples

Daily intakes of 12 phenols which are possible endocrine disruptors were estimated in hospital meals from 2000 to 2001. 4-Nonylphenol (4-NP (mix)) and bisphenol A (BPA) were detected at levels of 5.0 to 19.4 ng/g and 0.2 to 1.1 ng/g, respectively. 4-tert-Butylphenol, 4-n-pentylphenol, 4 -tert-pentylphenol, 4-n-hexylphenol, 4-n-heptylphenol and 4-tert-octylphenol were detected at levels of 0.1 to 2.4 microg/g. The daily intakes of 4-NP (mix) and BPA were 5.8 microg/day and 0.42 microg/day, respectively. The daily intakes of other phenols were less than 1 microg/day.     

Direct ethanol production from barley beta-glucan by sake yeast displaying Aspergillus oryzae beta-glucosidase and endoglucanase

Three beta-glucosidase- and two endoglucanase-encoding genes were cloned from Aspergillus oryzae, and their gene products were displayed on the cell surface of the sake yeast, Saccharomyces cerevisiae GRI-117-UK. GRI-117-UK/pUDB7 displaying beta-glucosidase AO090009000356 showed the highest activity against various substrates and efficiently produced ethanol from cellobiose. On the other hand, GRI-117-UK/pUDCB displaying endoglucanase AO090010000314 efficiently degraded barley beta-glucan to glucose and smaller cellooligosaccharides. GRI-117-UK/pUDB7CB codisplaying both beta-glucosidase AO090009000356 and endoglucanase AO090010000314 was constructed. When direct ethanol fermentation from 20 g/l barley beta-glucan as a model substrate was performed with the codisplaying strain, the ethanol concentration reached 7.94 g/l after 24 h of fermentation. The conversion ratio of ethanol from beta-glucan was 69.6% of the theoretical ethanol concentration produced from 20 g/l barley beta-glucan. These results showed that sake yeast displaying A. oryzae cellulolytic enzymes can be used to produce ethanol from cellulosic materials. Our constructs have higher ethanol production potential than the laboratory constructs previously reported.     

Expression of a gene encoding chitinase (pCA 8 ORF) from Aeromonas sp. no. 10S-24 in Escherichia coli and enzyme characterization

A gene encoding chitinase from Aeromonas sp. no. 10S-24 was expressed using pTrc99A in Escherichia coli JM 105 which yielded a 5-fold higher activity than when pUC19 was used. Three different truncated enzymes (SA-1, SA-2 and SA-3) were obtained after purification. Their isoelectric points were 7.0, 6.9, and 6.7, respectively. The enzymes showed two optimum pHs, 4.0 and 7.0, when incubated with ethylene glycol chitin as the substrate, and were stable over a wide pH range (3.0-9.0). The optimum temperature was 60 degrees C and the enzymes were stable up to 50 degrees C. The chitinases exhibited wide substrate specificities for chitin-related compounds.     

Debugging methods in recursive structured FORTRAN

A version of structured FORTRAN named STAR is introduced. STAR allows recursive subroutines. Implementation problems such as parameter passing by value and local variable stacking are discussed. The major difficulty in the preprocessor approach is debugging. We claim that execution profiles are strong debugging aids, and demonstrate how to debug a STAR program at source language level with the clue in the profiles plus assertion statements. We make use of a quicksort program as an example.     

Immobilization of mortierella vinacea cells by radiation polymerization

Immobilization of Mortierella vinacea cells, which contain active α-galactosidase, by radiation polymerization at low temperatures was studied. The durability of the enzymatic activity of the immobilized cells was examined by repeating the batch enzyme reaction. The enzymatic activities of the immobilized cells obtained with hydrophilic monomers was affected by the concentrations of the cells and monomer in which optimum conditions were observed. The enzymatic activity of the immobilized cells obtained with hydrophilic monomer was compared to that of hydrophobic monomers. Michaelis constants of the immobilized cells varied with monomer concentration. The effect of addition of porous solid substances on the immobilization of the cells was studied.