Optimization of Pectin Extraction from Melon Peel as a New Source of Pectin and Pectin Hydrolysate with Prebiotic Potential.

Food wastes have a large number of functional ingredients that have potential for valorization. Melon peels are increasingly produced as waste in food industries in Thailand. This study aimed to optimize pectin extraction conditions from melon peel for its prebiotic potential.

Association of natural resistance-associated macrophage protein 1 polymorphisms with fecal shedding and hematological traits in pigs.

Background And Aim: Natural resistance-associated macrophage protein 1 encoding gene () plays a role in immune response and disease resistance. This study aimed to investigate the polymorphisms of intron 6 concerning shedding and hematological traits in pigs.

Materials And Methods: A total of 40 commercial pigs (three-way Large White x Landrace x Duroc cross) were genotyped using the polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) method and analyze the relationship between the polymorphisms of the gene and fecal shedding and hematological parameters.

Structural insights into the unique polylactate-degrading mechanism of Thermobifida alba cutinase.

Cutinases are enzymes known to degrade polyester-type plastics. Est119, a plastic-degrading type of cutinase from Thermobifida alba AHK119 (herein called Ta_cut), shows a broad substrate specificity toward polyesters, and can degrade substrates including polylactic acid (PLA). However, the PLA-degrading mechanism of cutinases is still poorly understood.

Identification and in vitro assessment of potential probiotic characteristics and antibacterial effects of subsp SKI19, a bacteriocinogenic strain isolated from Thai fermented pork sausage.

A total of 2257 lactic acid bacteria were preliminarily screened for antagonistic activity against subsp. JCM 1157. Strain SKI19 was selected and identified at the subspecies level as subsp.

Comparison of genetic structures and biochemical properties of tandem cutinase-type polyesterases from Thermobifida alba AHK119.

This study described the genetic map of tandem genes (est1 and est119) encoding cutinase-type polyesterases in Thermobifida alba AHK119 and comparison of wild type and mutant enzymes of Est1 and Est119. Two genes were independently and constitutively expressed. The activity of Est1 was higher by approximately 1.

Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119.

Recombinant polyesterase (Est119) from Thermobifida alba AHK119 was purified by two chromatography steps. The final protein was observed as a single band in SDS-PAGE, and the specific activity of Est119 for p-nitrophenyl butyrate was 2.30 u/mg.

Diversity of polyester-degrading bacteria in compost and molecular analysis of a thermoactive esterase from Thermobifida alba AHK119.

More than 100 bacterial strains were isolated from composted polyester films and categorized into two groups, Actinomycetes (four genera) and Bacillus (three genera). Of these isolates, Thermobifida alba strain AHK119 (AB298783) was shown to possess the ability to significantly degrade aliphatic-aromatic copolyester film as well as decreasing the polymer particle sizes when grown at 50 degrees C on LB medium supplemented with polymer particles, yielding terephthalic acid. The esterase gene (est119, 903 bp, encoding a signal peptide and a mature protein of 34 and 266 amino acids, respectively) was cloned from AHK119.