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RISS 인기검색어
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- 저자 : Jorge Ariel Torres-Castillo (검색결과 2 건)
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Laura Jenet Montiel-Aguilar,Jorge Ariel Torres-Castillo,Rocío Rodríguez-Servin,Adiel Berenice López-Flores,Víctor Eustorgio Aguirre-Arzola,Gerardo Méndez-Zamora,Sugey Ramona Sinagawa-García 한국응용곤충학회 2020 Journal of Asia-Pacific Entomology Vol.23 No.3
Edible insects have been important sources of food proteins for human consumption and animal feed. In this study, a protein isolate from Pterophylla beltrani Bolivar & Bolivar, 1942 (Orthoptera: Tettigoniidae) was enzymatically processed and its nutraceutical properties were evaluated. Protein isolates were obtained from an insect flour and then was hydrolyzed for 5 h with a sequential process using pepsin and trypsin-chymotrypsin to simulate the gastric intestinal fluids. To evaluate the effect of peptide molecular size on nutraceutical properties, the peptides obtained from Total hydrolyzed (TH) were fractionated by ultrafiltration (UF) with 10 kDa and 3 kDa UF membranes giving fractions (F) with different molecular size (F < 3KDa, F < 10KDa and F > 10KDa). The inhibition assay of Angiotensin-Converting Enzyme (ACE) showed that the best treatment (P < 0.05) was the (TH) with an IC50 value of 0.5 mg/mL while the F < 3KDa was the lowest (P < 0.05) with an IC50 of 1.44 mg/mL, and the peptide size had no effect. However, an α-amylase inhibition was observed with an increase of the IC50 value between TH, F > 10KDa and F < 10KDa although no significative difference (P > 0.05) was found between the TH and F < 3KDa with IC50 of 0.48 and 0.68 mg/mL, respectively. In antioxidant activity, significant differences (P < 0.05) were observed between TH and UF fractions where the best response was in the F < 3KDa. In conclusion, P. beltrani proteins isolate are a source of bioactive peptide, and these could be considered as potential edible insect and sustainable food with nutraceutical effects.
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Edward Alexander Espinoza-Sanchez,Jorge Ariel Torres-Castillo,Quintın Rascon-Cruz,Francisco Zavala-Garcıa,Sugey Ramona Sinagawa-Garcıa 한국식물생명공학회 2016 Plant biotechnology reports Vol.10 No.2
The high capacity of the chloroplast genome to integrate and express transgenes at high levels makes transplastomic technology a good option for overexpressing proteins of interest. This report presents the stable expression of b-glucosidase (bgl1 gene) from Aspergillus niger and two cellulases (celA and celB genes) from Thermotoga neapolitana into the chloroplast genome of tobacco. The pES6, pHM4, pHM5 and pHM6 vectors were derived from the pES4 plasmid containing bgl1, celA-celB, celA and celB synthetic genes, respectively. All of the genes were flanked by a synthetic rrn16 promoter and the 30UTR from rbcL gene. The integration of the genes into intergenic regions rrn16 and 30rps12 of the inverted repeats was confirmed by Southern blot analysis. Stable expression and processing of monocistronic mRNA were confirmed by Northern blot analysis, and protein functionality was analysed via enzymatic activity assay. The recombinant enzymes exhibited high enzymatic activity at pH 5 (bglucosidase: 30.45 U mg-1 of TSP, celA-celB 58 U mg-1 of TSP, celA 49.10 U mg-1 of TSP and celB 48.72 U mg-1 of TSP). In addition, b-glucosidase exhibited high activity at 40 ℃, whereas cellulases type A (celA) and type B (celB) showed high activity at 65 ℃. NtpES6, NtpHM5 and NtpHM6 plants showed a similar phenotype compared with the wild type plants; however, NtpHM4 plants presented an abnormal phenotype with variegated leaves. This study, demonstrated that hydrolytic genes such as bgl1, celA and celB could be integrated and expressed correctly in the chloroplast genome. This work provides new information on methods and strategies for the expression of hydrolytic enzymes that are potentially useful for biotechnological applications using transplastomic plants.
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