• Title, Summary, Keyword: peptides

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Effects of Gluten and Soybean Polypeptides on Textural, Rheological, and Rehydration Properties of Instant Fried Noodles

  • Ahn, Chang-Won;Nam, Hee-Sop;Shin, Jae-Kil;Kim, Jae-Hoon;Hwan, Eun-Sun;Lee, Hyong-Joo
    • Food Science and Biotechnology
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    • v.15 no.5
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    • pp.698-703
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    • 2006
  • We investigated how the addition of polypeptides to instant fried noodle dough affects the dough properties, starch gelatinization, and textural properties of cup-type instant fried noodles. After comparing farinograph results of 100% wheat flour with 1% wheat flour substituted with gluten, there was a small difference in the mechanical dough properties. However, in the case of 1% wheat flour substituted with gluten peptides, the dough development time increased, dough stability decreased, and weakness increased. On the other hand, when gluten or gluten peptides were added, starch gelatinization did not change significantly. At the steaming stage, substitution with gluten peptides or soybean peptides markedly changed the molecular weight distributions of extractable polypeptides. Especially in the case of wheat flour substituted with 1% gluten peptides, the relative portion of low Mw extractable polypeptides (2.5-50 kDa) decreased more compared to a control. Also, the hardness and chewiness decreased in cooked cup-type instant fried noodles containing gluten peptides. This suggests that the addition of gluten peptides can reduce the rehydration time of cup-type instant fried noodles.

Structure-Antifungel Activity Relationships of Cecropin A Hybrid Peptides against Trichoderma sp.

  • Shin, Song-Yub;Lee, Dong-Gun;Lee, Sung-Gu;Kim, Kil-Lyong;Lee, Myung-Kyu;Hahm, Kyung-Soo
    • Journal of Microbiology
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    • v.35 no.1
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    • pp.21-24
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    • 1997
  • The hybrid peptides, CA-ME, CA-MA and CA-BO, with the N-terminal sequence 1-8 of cecropin A and the N-terminal sequences 1-12 of melittin, magainin 2 and bombinin, respectively, have more improved antibacterial activities. CA-MA was found to have stronger antifungal activity against Trichoderma sp than other hybrid peptides and their parental peptides. In order to elucidate the relationships between the peptide structure and antifungal activity, several analogues of CA-MA or CA-BO were also designed and synthesized by the solid phase method. An tifungal activity was measured against T. reesei and T. viride, and hemolytic activity was measured by a solution method against human red blood cells. The residue 16 of CA-MA, Ser, was found to be important for antifungal activity. When the residue was substituted with Leu, showed powerful antifungal activity was dramatically decreased. CA-MA, P1, P4 and P5 designed in this study showed powerful antifungal activity against T. reesei and T. viride with low hemolytic activity against human red blood cells. These hybrid peptides will be potentially useful model to further design peptides with powerful antifungal activity for the effective therepy of fungal infection and understand the mechanisms of antifungal actions of hybrid peptides.

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Calcium-binding Peptides Derived from Tryptic Hydrolysates of Cheese Whey Protein

  • Kim, S.B.;Lim, J.W.
    • Asian-Australasian Journal of Animal Sciences
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    • v.17 no.10
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    • pp.1459-1464
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    • 2004
  • The purpose of this research was to investigate the potential use of cheese whey protein (CWP), a cheese by-product. The physiological activity of calcium-binding peptides in CWP may be used as a food additive that prevents bone disorders. This research also examined the characteristics of calcium-binding peptides. After the CWP was heat treated, it was hydrolyzed by trypsin. Then calcium-binding peptides were separated and purified by ion-exchange chromatography and reverse phase HPLC, respectively. To examine the characteristics of the purified calcium-binding peptides, amino acid composition and amino acid sequence were analyzed. Calcium-binding peptides with a small molecular weight of about 1.4 to 3.4 kDa were identified in the fraction that was flowed out from 0.25 M NaCl step gradient by ion-exchange chromatography of tryptic hydrolysates. The results of the amino acid analysis revealed that glutamic acid in a calcium-binding site took up most part of the amino acids including a quantity of proline, leucine and lysine. The amino acid sequence of calcium-binding peptides showed Phe-Leu-Asp-Asp-Asp-Leu-Thr-Asp and Ile-Leu-Asp-Lys from $\alpha$-LA and Ile-Pro-Ala-Val-Phe-Lys and Val-Tyr-Val-Glu-Glu-Leu-Lys from ${\beta}$-LG.

Preparation and Characterization of Antioxidant Peptides from Fermented Goat Placenta

  • Hou, Yinchen;Zhou, Jiejing;Liu, Wangwang;Cheng, Yongxia;Wu, Li;Yang, Gongming
    • Food Science of Animal Resources
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    • v.34 no.6
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    • pp.769-776
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    • 2014
  • The goat placenta was fermented by Bacillus subtilis and the optimal fermentation parameters of strongest antioxidant capacity of peptides were obtained using response surface methodology (RSM). The effects of fermentation time, initial pH value and glucose content on the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging capacity of the goat peptides were well fitted to a quadric equation with high determination coefficients. According to the data analysis of design expert, the strongest DPPH radical scavenging capacity value was obtained with the following conditions: content of glucose was 2.23%, initial pH value was 7.00 and fermentation time was 32.15 h. The DPPH radical scavenging capacity commonly referring antioxidant activity showed a concentration dependency and increased with increasing peptide concentration. The effects of temperature and pH were assessed to determine the stability of antioxidant peptides prepared from goat placenta. Antioxidant peptides showed good stabilities when temperature was lower than $70^{\circ}C$. However, the antioxidant peptides lost antioxidant activities rapidly under alkaline and excessive acid condition. Ultrafiltration technique was performed to separate fermentation broth with different Mw (molecular weight). It was found that peptides in the range of < 3 KDa mainly accounted for the antioxidant activities.

The Use of Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) for Proteomics Research

  • Ng, Justin Tze-Yang;Hao, Piliang;Sze, Siu Kwan
    • Mass Spectrometry Letters
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    • v.5 no.4
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    • pp.95-103
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    • 2014
  • Characterization and studies of proteome are challenging because biological samples are complex, with a wide dynamic range of abundance. At present the proteins are identified by digestion into peptides, with subsequent identification of the peptides by mass spectrometry (MS). MS is a powerful technique for the purpose, but it cannot identify every peptide in such complex mixtures simultaneously. For accurate analysis and quantification it is important to separate the peptides first by chromatography into fractions of a size that MS can handle. With these less complex fractions, the probability is increased of identifying peptides of low abundance that would otherwise experience ion suppression effects due to the presence of peptides of high abundance. Enrichment for peptides with certain post-translational modifications helps to increase their detection rates as well. Electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) is a mixed-mode chromatographic technique which combines the use of electrostatic repulsion and hydrophilic interaction. This review provides an overview of ERLIC and its various proteomics applications. ERLIC has been demonstrated to have good orthogonality to reverse phase liquid chromatography (RPLC), making it useful as a first dimension in multidimensional liquid chromatography (MDLC) and fractionation of digests in general. Peptides elute in order of their isoelectric points and polarity. ERLIC has also been successfully utilized for the enrichment for phosphopeptides and glycopeptides, facilitating their identification. In addition, it is promising for the study of peptide deamidation. ERLIC performs comparably well or better than established methods for these various applications, and serves as a viable and efficient workflow alternative.

Mutant and Its Functional Revertant Signal Peptides of Escherichia coli Ribose Binding Protein Show the Differences in the Interaction with Lipid Bilayer

  • Oh, Doo-Byoung;Taeho Ahn;Kim, Hyoung-Man
    • Proceedings of the Korean Biophysical Society Conference
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    • pp.43-43
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    • 1999
  • Signal peptides of secretary proteins interact with various membranes and non-membrane components during the translocation. We investigated the interaction of signal peptides of ribose binding protein (RBP) with Escherichia coli (E.coli) signal recognition particle (SRP), SecA and lipid bilayer. Previous studies showed that the functional signal peptides inhibit the GTPase activity of E.coli SRP which consisted of F로 and 4.5S RNA.(omitted)

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Peptides-derived from Scales of Branchiostegus japonicus Inhibit Ultraviolet B-induced Oxidative Damage and Photo-aging in Skin Cells (피부세포에서 옥돔 비늘로부터 추출한 펩타이드의 UVB에 대한 산화적 손상 및 광 노화 억제)

  • Oh, Min Chang;Kim, Ki Cheon;Ko, Chang-ik;Ahn, Yong Seok;Hyun, Jin Won
    • Journal of Life Science
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    • v.25 no.3
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    • pp.269-275
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    • 2015
  • Collagen peptides, which are found at high concentrations in the human body, are present in animal bones and the skin of marine organisms, namely, fish scales. Collagen is the most abundant structural protein of various connective tissues in animals. Furthermore, it is widely used in biomedical material, pharmaceutical, cosmetic, food, and leather industries. Peptides extracted from scales of various fish protect against ultraviolet B (UVB)-induced skin damage and photo-aging. However, the protective effects of collagen peptides derived from the scales of Branchiostegus japonicus against UVB exposure are unclear. This study investigated the effects of peptides larger than 1 kDa (high-molecular weight peptides [HMP]) and smaller than 1 kDa (low-molecular weight peptides [LMP]), derived from extracts of B. japonicus scales, against UVB-induced skin damage and photo-aging. These peptides scavenged 1,1-diphenyl-2-picrylhydrazyl radicals in a dose-dependent manner. In UVB-exposed HaCaT human keratinocytes, LMP inhibited 8-isoprostane generation, a marker of cellular lipid peroxidation. The peptides also suppressed the UVB-induced increase in tyrosinase activity and melanin content in B16F10 mouse melanoma cells. In addition, the LMP and HMP treatment suppressed UVB-induced elastase and matrix metalloproteinase-1 activities in the HaCaT cells. These results indicate that peptides derived from B. japonicus scales have antioxidant, antiphoto-aging, and skin-whitening effects.

Isolation and identification of angiotensin I-converting enzyme inhibitory peptides derived from thermolysin-injected beef M. longissimus

  • Choe, Juhui;Seol, Kuk-Hwan;Kim, Hyun-Jin;Hwang, Jin-Taek;Lee, Mooha;Jo, Cheorun
    • Asian-Australasian Journal of Animal Sciences
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    • v.32 no.3
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    • pp.430-436
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    • 2019
  • Objective: This study identified angiotensin I-converting enzyme (ACE) inhibitory peptides in beef M. longissimus injected with thermolysin (80 ppm) and stored for 3 days at $5^{\circ}C$. Methods: Crude peptides (molecular weight <3 kDa) were obtained from the thermolysin hydrolysate and separated into seven fractions. Fraction V showing the highest ACE inhibitory activity was further fractionated, yielding subfractions V-15, V-m1, and V-m2, and selected for superior ACE inhibitory activity. Finally, twelve peptides were identified from the three peak fractions and the ACE inhibitory activity ($IC_{50}$) of each peptide was evaluated. Results: The Leu-Ser-Trp, Phe-Gly-Tyr, and Tyr-Arg-Gln peptides exhibited the strongest ACE inhibitory activity ($IC_{50}$ values of 0.89, 2.69, and 3.09 mM, respectively) and had higher concentrations (6.63, 10.60, and 29.91 pg/g; p<0.05) relative to the other peptides tested. Conclusion: These results suggest that the thermolysin injection process is beneficial to the generation of bioactive peptides with strong ACE inhibitory activity.

Isolation and Charaterization of Bioactive Peptides from Hwangtae (yellowish dried Alaska pollack) Protein Hydrolysate

  • Cho, San-Soon;Lee, Hyo-Ku;Yu, Chang-Yeon;Kim, Myong-Jo;Seong, Eun-Soo;Ghimire, Bimal Kumar;Son, Eun-Hwa;Choung, Myoung-Gun;Lim, Jung-Dae
    • Preventive Nutrition and Food Science
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    • v.13 no.3
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    • pp.196-203
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    • 2008
  • Hwangtae, dried Alaska pollack, is a major storage product in the fish processing industry. Hwangtae is prepared by removing the internal organs and drying outdoors during the cold witner months by allowing it to thaw during the daytime and re-freeze at night under sub-zero ($-10^{\circ}C$) conditions and gradually dry from December until the next April for around 5 months from Myungtae. In this study, ground Hwangtae was hydrolyzed using two proteolytic enzymes (pepsin and alcalase) which produced five soluble active peptides from Hwangtae (yellowish dried Pollack, Theragra chalcogramma) protein. Two different peptides with strong antioxidative activity were isolated from the hydrolysate using consecutive chromatographic methods of Sephadex G-25 gel, ion-exchange chromatography on a Sepharose-Sephadex C-25 gel, and high-performance liquid chromatography. The isolated peptides, APO1 and APO2, were composed of 16 and 13 amino acid residues, respectively. Both peptides contained a Gly residue at the C-terminus and the repeating motif Gly-Pro-Hyp. The peptide with a molecular weight less than 1,000 Daltons (APACE) obtained from enzymatic hydrolysates of Hwangtae exhibited the highest ACE inhibitory activity. The APACE peptides was composed of 4 amino acid residues (Gly-Leu-Leu-Pro). These results suggest that Hwangtae hydrolysates could be a good source of peptides with ACE inhibitory activity. Biochemical analysis indicated that two 70 kDa peptides (APG1 and APG2) isolated from the hydrolysate had gelatinoytic activity, which was shown to be a calcium dependent protease type as showed by gelatin SDS PAGE.

Identification of Antimicrobial Peptide Hexamers against Oral Pathogens through Rapid Screening of a Synthetic Combinatorial Peptide Library

  • Song, Je-Seon;Cho, Kyung Joo;Kim, Joungmok;Kim, Jeong Hee
    • International Journal of Oral Biology
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    • v.39 no.4
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    • pp.169-176
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    • 2014
  • A positional scanning synthetic peptide combinatorial library (PS-SCL) was screened in order to identify antimicrobial peptides against the cariogenic oral bacteria, Streptococcus mutans. Activity against Streptococcus gordonii and Aggregatibacter actinomycetemcomitans was also examined. The library was comprised of six sub-libraries with the format $O_{(1-6)}XXXXX-NH_2$, where O represents one of 19 amino acids (excluding cysteine) and X represents equimolar mixture of these. Each sub-library was tested for antimicrobial activity against S. mutans and evaluated for antimicrobial activity against S. gordonii and A. actinomycetemcomitans. The effect of peptides was observed using transmission electron microscopy (TEM). Two semi-mixture peptides, RXXXXN-$NH_2$ (pep-1) and WXXXXN-$NH_2$ (pep-2), and one positioned peptide, RRRWRN-$NH_2$ (pep-3), were identified. Pep-1 and pep-2 showed significant antimicrobial activity against Gram positive bacteria (S. mutans and S. gordonii), but not against Gram negative bacteria (A. actinomycetemcomitans). However, pep-3 showed very low antimicrobial activity against all three bacteria. Pep-3 did not form an amphiphilic ${\alpha}$-helix, which is a required structure for most antimicrobial peptides. Pep-1 and pep-2 were able to disrupt the membrane of S. mutans. Small libraries of biochemically-constrained peptides can be used to generate antimicrobial peptides against S. mutans and other oral microbes. Peptides derived from such libraries may be candidate antimicrobial agents for the treatment of oral microorganisms.