Search Results

You are looking at 1 - 3 of 3 items for :

  • Author or Editor: E. Takács x
  • Biology and Life Sciences x
  • Refine by Access: Content accessible to me x
Clear All Modify Search

Apple is one of the most important fruit grown and consumed in the temperate climate region. About 2% of the European population suffers from several allergenic reactions after consumption. Presence of 7 members of Mal d 1 gene family occurring in some apples was examined by PCR. The Mal d 1.01 and 1.02 genes could be detected from 91% and 79% of apple cultivars, respectively, due to the high degree of conservative regions. The Mal d 1.04 gene has 4 functional varieties and 2 pseudo-alleles, so it is highly variable. The PCR amplifi cation with Mal d 1.06 primers gave one or two fragments with different sizes. The electrophoretic pattern is a suitable means to select apple cultivars according to their low, medium, or high Mal d 1 allergen content. Florina apple showed the single 154 bp allele, which is responsible for the small Mal d 1 allergen content in homozygote form..

Several samples gave weak signal or did not give any fragment-band on the gel, so Mal d 1.07 and 1.08 genes might have more varieties. Regarding the Mal d 1.09 gene we have found that it has conservative sequences in different apple cultivars and does not have too many varieties.

Open access

Abstract

Enzymatic hydrolysates of mechanically deboned meat (MDM) for a long time have been used as flavouring and functional food ingredients in the food industry and also as the bases of formula foods for special dietary uses.

The aim of the present study was to produce MDM hypo-antigenic products with improved digestibility and high biological value to be used as a milk protein alternative. turkey MDM was treated with digestive enzymes (trypsin and/or α-chymotrypsin, or pancreatin), followed by freeze drying. The optimised reaction conditions of hydrolysis were at 6% (w/v) of meat protein in 0.1% NaHCO3 buffer, pH 7.5; pancreatin enzyme with 50 TAME units/g meat protein substrate, 37 °C and 60 min). Hydrolysates (MDMH) were assessed for degree of hydrolyses (DH, %) by using trinitrobenzenesulphonic acid method and MW distribution by SDS-PAGE. Modification of immune reactive binding sites in MDMHs was monitored by immunoblot with cow’s milk, chicken egg or meat allergic human patients’ sera. Biological value indices (True Digestibility (TD), Net Protein Utilisation (NPU), Biological Value (BV)) were determined using rat feeding trials. Among the MDMH products, the pancreatic hydrolysate proved to be the most favourable in terms of biological value and digestibility as well as hypoallergenic property.

Open access
Acta Alimentaria
Authors:
E. Horvath-Szanics
,
J. Perjéssy
,
A. Klupács
,
K. Takács
,
A. Nagy
,
E. Koppány-Szabó
,
F. Hegyi
,
E. Németh-Szerdahelyi
,
M.Y. Du
,
Z.R. Wang
,
J.Q. Kan
, and
Zs. Zalán

The increasing consumer demand for less processed and more natural food products – while improving those products’ quality, safety, and shelf-life – has raised the necessity of chemical preservative replacement. Biopreservation refers to extended storage life and enhanced safety of foods using the natural microflora and (or) their antibacterial products. Chitinolytic enzymes are of biotechnological interest, since their substrate, chitin, is a major structural component of the cell wall of fungi, which are the main cause of the spoilage of food and raw plant material. Among the several organisms, many bacteria produce chitinolytic enzymes, however, this behaviour is not general. The chitinase activity of the lactic acid bacteria is scarcely known and studied.

The aim of the present study was to select Lactobacillus strains that have genes encoding chitinase, furthermore, to detect expressed enzymes and to characterise their chitinase activity. Taking into consideration the importance of chitin-bindig proteins (CBPs) in the chitinase activity, CBPs were also examined. Five Lactobacillus strains out of 43 strains from 12 different species were selected by their chitinase coding gene. The presence of the chitinase and chitin-biding protein production were confirmed, however, no chitinolytic activity has been identified.

Open access