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1.
3 Biotech ; 10(3): 115, 2020 Mar.
Article in English | MEDLINE | ID: mdl-32117676

ABSTRACT

In the present study, a potential newly isolated thermotolerant acetic acid bacteria (TH-AAB), Acetobacter pasteurianus FPB2-3, with ethanol and acetic acid-tolerant properties was found to be very effective in the production of vinegar from pineapple peels as an alternative, inexpensive raw material using simultaneous vinegar fermentation (SVF). The results showed that using whole pineapple peel with the addition of diammonium phosphate (DAP) and MgSO4 at an initial pH of 5.5 gave a slightly higher acetic acid content than that produced from the squeezed juice. Subsequently, the effects of sugar concentration and inoculation time of A. pasteurianus FPB2-3 on acetic acid production were examined. The results revealed that an increase in sucrose concentration led to the high production of ethanol, which resulted in the suppression of acetic acid production. Allowing for the inoculated yeast to ferment prior to inoculation of the AAB for 1 or 2 days resulted in a longer lag time for ethanol oxidation. However, acetic acid accumulation commenced after 5 days and gradually increased to the maximum concentration of 7.2% (w/v) within 16 days. Furthermore, scaled-up fermentation in 6 l vessels resulted in slower acetic acid accumulation but still achieved a maximum acetic acid concentration of up to 6.5% (w/v) after 25 days. Furthermore, the antioxidant capacity of the vinegar produced from pineapple peels (PPV) was slightly higher than that produced from the squeezed juice (PJV), which was consistent with the higher total phenolic compound content found in the PPV sample. In addition to acetic acid, a main volatile acid present in vinegars, other volatile compounds, such as alcohols (isobutyl alcohol, isoamyl alcohol, and 2-phenyl ethanol), acids (3-methyl-butanoic acid), and esters (ethyl acetate, 3-methyl butanol acetate, and 2-phenylethyl acetate), were also detected and might have contributed to the observed differences in the odour and aroma of the pineapple vinegars.

2.
BMC Plant Biol ; 8: 84, 2008 Jul 30.
Article in English | MEDLINE | ID: mdl-18664295

ABSTRACT

BACKGROUND: Many plant beta-galactosidases (Bgals) have been well characterized and their deduced biological functions mainly involve degradation of structural pectins, xyloglucans or arabinogalactoproteins in plant cell walls. However, gene multiplicity in glycosyl hydrolase family 35 (GH35), to which these proteins belong, implies diverse functions. In this study, the gene multiplicity, apparent evolutionary relationships and transcript expression of rice Bgal genes were examined, in order to predict their biological functions. RESULTS: Fifteen rice Bgal genes were identified in the plant genome, one of which encodes a protein similar to animal Bgals (OsBgal9), and the remaining 14 fall in a nearly plant-specific subfamily of Bgals. The presence of both classes of Bgals in bryophytes, as well as vascular plants, suggests both gene lineages were present early in plant evolution. All 15 proteins were predicted to contain secretory signal sequences, suggesting they have secretory pathway or external roles. RT-PCR and database analysis found two distinct lineages to be expressed nearly exclusively in reproductive tissues and to be closely related to Arabidopsis Bgals expressed most highly in flower and pollen. On the other hand, OsBgal6 is expressed primarily in young vegetative tissues, and alternative splicing in panicle prevents its production of full-length protein in this reproductive tissue. OsBgal11 also showed alternative splicing to produce different length proteins. OsBgal13 produced by recombinant expression in Escherichia coli hydrolyzed alpha-L-arabinoside in addition to beta-D-galactoside and beta-(1-->3)-, beta-(1-->4)- and beta-(1-->6)- linked galacto-oligosaccharides. CONCLUSION: Rice GH35 contains fifteen genes with a diversity of protein sequences, predicted locations and expression and splicing patterns that suggest that OsBgals enzymes may play a variety of roles in metabolism of cell wall polysaccharides, glycoproteins and glycolipids.


Subject(s)
Gene Expression Regulation, Plant , Genes, Plant , N-Glycosyl Hydrolases/genetics , Oryza/enzymology , Oryza/genetics , Alternative Splicing/genetics , Chromosomes, Plant/genetics , DNA, Complementary/genetics , Exons/genetics , Glycosides/metabolism , Hydrolysis , Introns/genetics , Isoenzymes/genetics , Isoenzymes/metabolism , Oligosaccharides/metabolism , Phylogeny , Plant Proteins/genetics , Plant Proteins/metabolism , Retroelements/genetics , Reverse Transcriptase Polymerase Chain Reaction , Sequence Analysis, DNA , Sequence Homology, Nucleic Acid , beta-Galactosidase/genetics , beta-Galactosidase/metabolism
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