• Title/Summary/Keyword: proteolytic conditions

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Conditions for the Production of Amylase and Pretense in Marking Wheat Flour Nuluk by Aspergillus usamii mut. shirousamii S1 (Aspergillus usamii mut. shirousamii S1에 의한 밀가루누룩 제조시 Amylase와 Pretense의 생산조건)

  • 오명환;박서영
    • The Korean Journal of Food And Nutrition
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    • v.7 no.1
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    • pp.51-57
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    • 1994
  • A nuluk, a Korean traditional koji for brewing, was made with wheat flour and Aspergillus usamii mot. shirousamii S1 which had strong abilities in producing amylase and protease. The cultural conditions for the production of saccharogenic and proteolytic enzymes were tested. The productivities of saccharogenic and dextrogenic enzymes were improved when nuluk was made with unsteamed wheat flour as compared with steamed one, but those of proteolytic enzyme and organic acid were reduced. The addition of water containing 0.5% of hydrochloric acid was unfavorable for the production of saccharogenic, dextrogenic and proteolytic enzymes. The optimum ratios of water added to wheat flour for the production of saccharogenic enzyme and proteolytic enzyme were 32% and 28%, respectively on the basis of wheat flour. The optimum temperatures for the production of saccharogenic enzyme and proteolytic enzyme were 36$^{\circ}C$ and 28$^{\circ}C$, respectively. The activity of saccharogenic enzyme reached its maximum after 120 hours of cultivation at 36$^{\circ}C$, but that of proteolytic enzyme 96 hours. The productivity of saccharogenic enzyme was enhanced when the nuluk was molded after 24 hours of precultivation but that of proteolytic enzyme was reduced as compared with no molding.

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Expression, Refolding, and Characterization of the Proteolytic Domain of Human Bone Morphogenetic Protein 1 (뼈형성 단백질(Bone Morphogenetic Protein 1)의 단백질 분해 부위의 발현 및 특성 연구)

  • ;Daihung Do
    • Journal of Life Science
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    • v.10 no.2
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    • pp.218-227
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    • 2000
  • Bone morphogenetic protein 1 (BMP-1) is part of a complex capable of inducing ectopic bone formation in mammals. Studies on TGF-β1 processing and Drosophila dorsal-ventral patterning have focused attention on BMP-1 as important in mediating the biological activity of this bone inducing complex. Herein, the bacterial expression, refolding, purification, and initial characterization of the BMP-1 proteolytic domain (BPD) are described. A semi-quantitative fluorescence-based thin layer chromatography assay was developed to assist in rapidly screening for optimal renaturation conditions. According to a preliminary screen for optimal conditions for the refolding of BPD , a detectable proteolytic activity against a high turnover substrate for astacin, a homologous protease from crayfish was observed. The conditions identified have allowed the expression of sufficient amounts of BPD for the characterization of the protein. Its proteolytic activity exhibits the same cleavage specificity as astacin against seven substrates that were previously synthesized for studying astacin. Furthermore, this activity is inhibited by the metal chelator 1,10-phenanthroline but not by its analogue 1,7-phenanthroline. The collagenase inhibitor Pro-Leu-Gly hydroxamate was found to inhibit both astacin and BPD activity. The results presented in this paper argue that BMP-1 does in fact possess an intrinsic proteolytic activity.

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The Growth of Proteolytic Bacteria Immobilized in Capsule Type

  • Han Bong-Ho;Choi Su-Il;Kim Seong-Bong;Kim Sang-Ho
    • Fisheries and Aquatic Sciences
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    • v.2 no.1
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    • pp.44-51
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    • 1999
  • Proteolytic bacteria isolated from fermented anchovy jeotkal were immobilized in capsule type with $0.8\%$ sodium alginate and $CaCl_2/carboxymethyl$ cellulose (CMC). For making the immobilized capsule, the optimal concentration of both $CaCl_2$ and CMC, with respect to the membrane hardness and the growth of proteolytic bacteria in capsule, were $2.0\%$ at following conditions: flow rate of $CaCl_2/CMC$ solution and cell suspension were respectively 3.54 ml/min and 0.15 ml/min when inside diameter of inner and outer capillary tube in immobilizing apparatus were 0.32mm, 0.74mm, respectively. The density of proteolytic bacteria in capsule reached maximum, i.e. $10^8-10^9cells$/capsule during culture under optimal conditions in TPY broth, and these were $10^2-10^4$ times higher than these of before culture. During culture of proteolytic bacteria immobilized in capsule type (PBImC) for 72hrs, few growing cells were lost in the outer medium.

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Conditions for the Production of Amylase and Protease in Making Wheat Flour Nuluk by Aspergillus oryzue L2 (Aspergillus oryzae L2에 의한 밀가루 누룩 제조시 Amylase와 Pretense의 생산조건)

  • 오명환
    • The Korean Journal of Food And Nutrition
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    • v.6 no.2
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    • pp.89-95
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    • 1993
  • A Nuluk, a Korean traditional Koji for brewing, was made with wheat flour and Aspergillus oryzae L2 which had a good aroma and strong abilities In producing saccharogenic and dextrogenic enzymes. The cultural conditions for the production of saccharogenic and proteolytic enzymes were tested. The productivity of dextrogenic enzyme was improved when Nuluk was made with unsteamed wheat flour as compared with steamed one, but that of proteolytic enzyme was reduced. The addition of water containing 0.5% hydrochloric acid was unfavorable for the production of those two enzymes. The optimum ratio of water added to wheat flour for the production of those two enzymes was 28$^{\circ}C$ on the basis of wheat flour, The productivity of saccharogenic enzyme was enhanced when the Nuluk was molded after 20 hours of precultivation, but that of proteolytic enzyme was reduced as compared with no molding. The optimum temperatures for the production of saccharogenic enzyme and proteolytic enzyme were 36$^{\circ}C$ and 28$^{\circ}C$, respectively.

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Conditions for the Production of Amylase and Protease in Making Wheat flour Nuluk by Rhizopus japonicas T2 (Rhizopus japonicus T2에 의한 밀가루 누룩 제조시 Amylase와 Protease의 생산조건)

  • 소명환
    • The Korean Journal of Food And Nutrition
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    • v.6 no.2
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    • pp.96-102
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    • 1993
  • A Nuluk, a Korean traditional koji for brewing, was made with wheat flour and Rhizopus japonicus T2 which had a good aroma and strong abilities in producing saccharogenic and proteolytic enzymes, and cultural conditions for the production of those two enzymes were tested. The productivity of saccharogenic enzyme was markedly improved when Nuluk was made with unsteamed wheat flour as compared with that with steamed one, but that of acid protease was reduced. The addition of water containing 0.5% hydrochloric acid was unfavorable for the production of saccharogenic enzyme and neutral protease. The optimum ratio of water added to wheat flour for the production of saccharogenic enzyme and proteolytic enzyme was 28% on the basis of wheat flour. The productivity of saccharogenic enzyme was enhanced "when the Nuluk was molded after 10~20 hours precultivation but that of proteolytic enzyme was reduced as compared with no molding. The optimum temperature for the production of saccharogenic enzyme was 28f and that of proteolyic enzyme was also 28$^{\circ}C$. The optimum cultural time for the production of saccharogenic enzyme was 36 ~72 hours at 3$0^{\circ}C$ and that of proteolytic enzyme was 36 hours.ours.

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Endogenous Proteolytic Systems and Meat Tenderness: Influence of Post-Mortem Storage and Processing

  • Kaur, Lovedeep;Hui, Seah Xin;Morton, James D.;Kaur, Ramandeep;Chian, Feng Ming;Boland, Mike
    • Food Science of Animal Resources
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    • v.41 no.4
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    • pp.589-607
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    • 2021
  • Meat proteolytic systems play a crucial role in meat tenderisation. Understanding the effects of processing technologies and post-mortem storage conditions on these systems is important due to their crucial role in determining the quality characteristics of meat and meat products. It has recently been proposed that tenderisation occurs due to the synergistic action of numerous endogenous proteolytic systems. There is strong evidence suggesting the importance of μ-calpain during the initial post-mortem aging phase, while m-calpain may have a role during long-term aging. The caspase proteolytic system is also a candidate for cell degradation in the initial stages of conversion of muscle to meat. The role of cathepsins, which are found in the lysosomes, in post-mortem aging is controversial. Lysosomes need to be ruptured, through aging, or other forms of processing to release cathepsins into the cytosol for participation in proteolysis. A combination of optimum storage conditions along with suitable processing may accelerate protease activity within meat, which can potentially lead to improved meat tenderness. Processing technologies such as high pressure, ultrasound, and shockwave processing have been reported to disrupt muscle structure, which can facilitate proteolysis and potentially enhance the aging process. This paper reviews the recent literature on the impacts of processing technologies along with post-mortem storage conditions on the activities of endogenous proteases in meat. The information provided in the review may be helpful in selecting optimum post-mortem meat storage and processing conditions to achieve improved muscle tenderness within shorter aging and cooking times.

A Study on the Optimum Conditions of Gelatin-Degrading Proteolytic Enzyme Production from Bacillus subtilis B0021 (Bacillus subtilis B0021가 생산하는 Gelatin 분해성 Proteolytic Enzyme 생산의 최적의 연구)

  • 백대헌;이항우복성해
    • KSBB Journal
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    • v.10 no.4
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    • pp.374-385
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    • 1995
  • Nutritional requirements and cultural conditions for the production of extracellular gelatin-degrading proteolytic enzyme by Bacillus subtilis B0021 were investigated. Optimum carbon source for proteolytic enzyme production was salicin, but it was substituted by glucose for economical reason. The fermentation medium giving a maximum proteolytic enzyme activity was consisted of 1.5%(w/v) glucose, 2.5%(w/v) yeast extract, and 0.001%(w/v) manganese sulfate and 0.002%(w/v) ferrous sulfate. Proteolytic enzyme activity of B. subtilis B0021 was completely inhibited by 0.5%(w/v) tannic acid. Initial pH was optimal at 7.0 and the enzyme activity in the flask culture usually reached a maximal level after 36 hours of fermentation at $30^{\circ}C$. In the $5\ell$ fermentor fermentation at $30^{\circ}C$, enzyme activity was maximum at 36 hour of cultivation but after this enzyme activity was decreased rapidly. Initial viscosity of 45%(w/v) gelatin(2,800mPas) was decreased rapidly to 96%(mPas) after hydrolysis for 4hr at $40^{\circ}C$ by crude enzyme of B. subtilis B0021.

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Degradation Characteristics of A Novel Multi-Enzyme-Possessing Bacillus licheniformis TK3-Y Strain for the Treatment of High-Salinity Fish Wastes and Green Seaweeds

  • Kang, Kyeong Hwan;Kim, Joong Kyun
    • Fisheries and Aquatic Sciences
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    • v.18 no.4
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    • pp.349-357
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    • 2015
  • To reutilize fisheries waste, we isolated a bacterial strain from a coastal area located in Busan. It was identified as Bacillus licheniformis TK3-Y. Using plate assay and 500-mL flask experiments, we found that the isolate simultaneously possessed cellulolytic, proteolytic, and lipolytic activities with salt tolerance. 10% (v/v) inoculums, were used to examine the biodegradation characteristics of the TK3-Y strain on carboxymethylcellulose, skim milk, and olive oil media. The optimum conditions for pH, temperature, agitation speed, and NaCl concentration on each 1% substrate were 6, $50^{\circ}C$, 180 rpm, and 17.5%, respectively. Under optimal conditions, the TK3-Y strain showed 1.07 U/mL cellulolytic, 1,426 U/mL proteolytic, and 6.45 U/mL lipolytic activities. Each enzyme was stable within a range of 17.5-35% NaCl. Therefore, the salt tolerance ability of strain TK3-Y was superior to other related strains. In degradation of a mixed medium containing all three substrates, both the cellulolytic and proteolytic activities were somewhat lower than those on each single substrate, while the lipolytic activity was somewhat higher. From the above results, the TK3-Y strain appears to be a good candidate for use in the efficient treatment of fisheries waste in which components are not collected separately.

Potential of proteolytic enzyme treatment for production of Korean red ginseng extract (홍삼 추출물의 제조에서 단백질 분해효소의 활용)

  • Kim, Dong Chung;Lee, Tae Jung;In, Man-Jin
    • Journal of Applied Biological Chemistry
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    • v.62 no.4
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    • pp.385-389
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    • 2019
  • In this study, proteolytic enzymatic treatment conditions for Korean red ginseng were examined to increase the extraction yield. Commercially available proteases were screened to obtain high protein and carbohydrate yield. The optimal dosage and reaction time for Alcalase, the chosen protease, were found to be 2.0% (w/w) and 1.5 h, respectively. Treatment with optimal conditions of Alcalase increased solid yield, total phenolic content and gensenosides content by 57.6, 81.8, and 33.8%, respectively, over levels in non-treated Korean red ginseng. Antioxidative activities evaluated by free radical scavenging activity, cation radical scavenging activity and reducing power were exactly similar between Alcalase-treated and non-treated extracts.

Preparation of Oyster (Crassostrea gigas) and Sea Mussel (Mytilus coruscus) Hydrolyzates using Commercial Protease (단백질 분해효소를 이용한 굴과 홍합 가수분해물의 제조)

  • Lee, Young-Chul;Kim, Dong-Soo;Kim, Young-Dong;Kim, Young-Myoung
    • Korean Journal of Food Science and Technology
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    • v.22 no.3
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    • pp.234-240
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    • 1990
  • Attempts have been made to optimize the hydrolysis conditions of the oyster and the mussel by the commercial proteolytic enzymes. Raw materials were digested with seven different commercial enzymes, and their quality parameters measured in terms of degree of hydrolysis and content of free amino nitrogen, nucleic acid-related substances. and free amino acids as well as sensory evaluation of optimization of their hydrolysis conditions. As a result, following enzymes have been disclosed as effective for enzymatic digestion: MKC-HT proteolytic, alcalase 0.6L and thermease for the oyster whereas MKC-acid fungal protease and thermoase for the mussel, respectively.

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