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      • KCI등재

        Cities as Place for Climate Mitigation and Adaptation : A Case Study of Portland, Oregon, USA

        Heejun Chang(장희준),Lily House-Peters 대한지리학회 2010 대한지리학회지 Vol.45 No.1

        도시는 적극적으로 온실가스배출을 저감하고 기후변화에 대한 적응전략을 구현할 수 있는 적합한 장소이다. 기존의 도시 기후 변화 완화와 적응의계획, 정책, 이행에 관한 연구를 지속가능성 과학, 세계변화 과학, 다차원 거버넌스, 구조공학의 네가지 범주로 나누어 고찰하였다. 이 네가지 학문은 관점이 서로 다르지만 모두 기후변화로 인해 야기될 수 있는 위협을 극복하는데 보편적인 주제를 공유하고 있다. 포트랜드 시의 사례연구는 도시가 현명한 성장, 국지적인 기후대응 계획, 다차원 규모의 거버넌스, 녹생성장에 기여하는 그린 인프라구조의 설치등을 통해 온실가스를 저감하고 기후변화에 능동적으로 대응할 수 있음을 제시한다. 더욱이 도시에 위치한 대학은 민간과 공공부문의 다양한 조직을 연결하고, 혁신적인 연구센터와 공간적으로 명확한 그린 인프라스트럭처를 창출하며, 영향평가 방법과 캠퍼스 탄소 인벤토리를 구축하며, 서비스 학습을 통해 학생과 커뮤너티를 연결하여 이러한 기후변화의 완화와 대응의 허브로서 작용할 수 있다. Cities are major sources of greenhouse gas emissions but also suitable places for implementing proactive climate mitigation and adaptation strategies. Based on the interdisciplinary review of literature, we categorize the current discussion about urban climate mitigation and adaptation planning, policy and practices into four perspectives - sustainability science, global change science, multilevel governance, and structural engineering. While these four schools of thought have distinct perspectives rooted in different disciplinary lenses, our synthesis of the literature identifies several universal themes that are common to all of the perspectives in the context of combating threats posed by climate change. The Portland case study illustrates that a city can make changes to reduce greenhouse gas emissions and increase adaptive capacity to climate change impacts by implementing smart growth, devising local climate action plans that target emission reductions in various sectors, recognizing the interactions and influences of multiple scales of governance, and supporting the installation of various green infrastructures that contribute to green economy. Furthermore, a university can serve as a hub in this climate mitigation and adaptation arena by connecting various levels of community organizations in both public and private sectors, creating innovative research centers and spatiallyexplicit green infrastructure, designing impact assessments and campus carbon inventories, and engaging students and the larger community through service learning.

      • SCIESCOPUSKCI등재

        Effect of Mutagenesis of V111 and L112 on the Substrate Specificity of Zymomonas mobilis Pyruvate Decarboxylase

        (Chang Yi Huang),(Peter F . Nixon),(Ronald G . Duggleby) 생화학분자생물학회 1999 BMB Reports Vol.32 No.1

        Pyruvate decarboxylase (PDC) catalyzes the conversion of pyruvate to acetaldehyde as the penultimate step in alcohol fermentation. The enzyme requires two cofactors, thiamin diphosphate (ThDP) and Mg^(2+), for activity. Zymomonas mobilis PDC shows a strong preference for pyruvate although it will use the higher homologues 2-ketobutyrate and 2-ketovalerate to some extent. We have investigated the effect of mutagenesis of valine 111 and leucine 112 on the substrate specificity. V111 was replaced by glycine, alanine, leucine, and isoleucine while L112 was replaced by alanine, valine, and isoleucine. With the exception of L1121, all mutants retain activity towards pyruvate with k_cat values ranging from 40% to 139% of wild-type. All mutants show changes from wild-type in the affinity for ThDP, and several (V111A, L112A, and L112V) show decreases in the affinity for Mg ^(2+). Two of the mutants, V111G and V111A, show an increase in the K_m for pyruvate. The activity of each mutant towards 2-ketobutyrate and 2-ketovalerate was investigated and some changes from wild-type were found. For the V111 mutants, the most notable of these is a 3.7-fold increase in the ability to use 2-ketovalerate. However, the largest effect is observed for the L112V mutation which increases the ability to use both 2-ketobutyrate (4.3-fold) and 2-ketovalerate (5.7-fold). The results suggest that L112 and, to a lesser extent, V111 are close to the active site and may interact with the alkyl side-chain of the substrate.

      • KCI등재

        Replacement value of cassava for maize in broiler chicken diets supplemented with enzymes

        Chang'a Edwin Peter,Abdallh Medani Eldow,Ahiwe Emmanuel Uchenna,Mbaga Said,Zhu Ze Yuan,Fru-Nji Fidelis,Iji Paul Ade 아세아·태평양축산학회 2020 Animal Bioscience Vol.33 No.7

        Objective: Pellet durability, particle size distribution, growth response, tibia bone characteristics and energy retention were measured to evaluate cassava as an alternative energy source to replace maize in broiler diets with or without Ronozyme (A+VP) enzyme composites. Methods: A total of 480 one-day broiler chicks were randomly assigned to 8 treatments in a 4×2 factorial arrangement. Four levels of cassava: (0%, 25%, 50%, 75%) and 2 levels of enzymes (0 and 500 g/tonne) were used. Each treatment was replicated six times, with ten birds per replicate. Results: The particle size distribution in the diets showed an increasing trend of small particles with increase in cassava level. Pellet durability decreased (p<0.05) with cassava inclusion. Feed intake was highest in birds fed diets with medium cassava level at 1 to 24 d and 1 to 35 d of age. The body weight gain of birds reduced (p<0.037) as cassava level increased, but it increased (p<0.017 when enzymes were added. The feed conversion ratio was high (p<0.05) when cassava level was increased, but it reduced (p<0.05) when enzymes were added. The dressing percentage (DP), and weight of drumsticks reduced (p<0.05) with increasing cassava level. Enzyme supplementation increased (p<0.05) DP, and weight of breast, thighs and drumsticks. Ash content, weight, length, width, and bone strength decreased (p<0.05) when cassava level was increased, however, they were increased with enzyme addition. The contents of Ca, K, and Zn were raised (p<0.001) with increasing cassava level. Enzyme inclusion increased (p<0.001) all mineral contents in tibia bones. Body fat and energy retained as fat decreased (p<0.001) as cassava level increased. Enzyme inclusion increased (p<0.05) body protein content and energy retained as protein. Conclusion: Although broiler performance was depressed by high levels of cassava inclusion, it was not affected by low levels, which further improved by enzyme supplementation.

      • KCI우수등재

        Energy utilization, nutrient digestibility and bone quality of broiler chickens fed Tanzania-type diets in different forms with enzymes

        ( Edwin Peter Chang’a ),( Medani Eldow Abdallh ),( Emmanuel Uchenna Ahiwe ),( Mohammed Al-qahtani ),( Said Mbaga ),( Paul Ade Iji ) 한국축산학회 2019 한국축산학회지 Vol.61 No.4

        A study was conducted to determine the influence of feed form and microbial enzyme supplementation on energy utilization, bone quality, and amino acid and mineral digestibility of broiler chickens. Four hundred and eighty Ross 308, day-old broiler chickens were randomly assigned to eight diets formulated from commonly used ingredients in Tanzania. A 2 (pellet or mash) × 4 (control, Axtra XB, Quantum Blue (QB) and Axtra XB + QB enzyme) factorial array in a completely randomized design having six replicates per treatment (10 birds per replicate) was used. Birds were raised in climate-controlled rooms in a 3-phase; starter (0-10 days), grower (11-24 days) and finisher (25-35 days). Apparent metabolizable energy (AME), metabolizable energy intake, net energy of production, energy retained as protein (REp), and efficiency of metabolizable energy use for energy and protein retention were higher (p < 0.05) in birds fed pelleted diets. The AME and REp was higher (p < 0.05) with enzyme supplementation. Ash content, weight, length, width and breaking strength of tibia bones were highest (p < 0.05) in birds on pelleted diets. Tibia bone traits were improved (p < 0.05) when enzymes were included, particularly in a combination of QB and Axtra XB. However, potassium, magnesium, and zinc contents were highest (p < 0.05) when QB was supplemented. Digestibility of all amino acids was higher (p < 0.05) in birds supplied with pellets and with enzyme supplementation for most amino acids, except for serine. There was a positive interaction (p < 0.05) between feed form and enzymes on lysine and phenylalanine digestibility. Digestibility of Ca, P, K, S, Zn, and Fe was higher (p < 0.05) in birds fed pelleted diets, while those on mashed diets had higher (p < 0.05) digestibility of Cu and B. The digestibility of P, K, and Zn was highest (p < 0.001) when QB was added, while Ca, P, S, and B digestibility was highest when a combination of Axtra XB + QB was applied. Pelleted diets with or without enzymes improved energy utilization, digestibility of amino acids, and minerals, and increased bone strength in broiler chickens.

      • Effect of Mutagenesis of V111 and L112 on the Substrate Specificity of Zymomonas mobilis Pyruvate Decarboxylase

        Huang, Chang-Yi,Nixon, Peter F.,Duggleby, Ronald G. Korean Society for Biochemistry and Molecular Biol 1999 Journal of biochemistry and molecular biology Vol.32 No.1

        Pyruvate decarboxylase (PDC) catalyzes the conversion of pyruvate to acetaldehyde as the penultimate step in alcohol fermentation. The enzyme requires two cofactors, thiamin diphosphate (ThDP) and $Mg^{2+}$, for activity. Zymomonas mobilis PDC shows a strong preference for pyruvate although it will use the higher homologues 2-ketobutyrate and 2-ketovalerate to some extent. We have investigated the effect of mutagenesis of valine 111 and leucine 112 on the substrate specificity. V111 was replaced by glycine, alanine, leucine, and isoleucine while L112 was replaced by alanine, valine, and isoleucine. With the exception of L112I, all mutants retain activity towards pyruvate with $k_{cat}$ values ranging from 40% to 139% of wild-type. All mutants show changes from wild-type in the affinity for ThDP, and several (V111A, L112A, and L112V) show decreases in the affinity for $Mg^{2+}$. Two of the mutants, V111G and V111A, show an increase in the $K_m$ for pyruvate. The activity of each mutant towards 2-ketobutyrate and 2-ketovalerate was investigated and some changes from wild-type were found. For the V111 mutants, the most notable of these is a 3.7-fold increase in the ability to use 2-ketovalerate. However, the largest effect is observed for the L112V mutation which increases the ability to use both 2-ketobutyrate (4.3-fold) and 2-ketovalerate (5.7-fold). The results suggest that L112 and, to a lesser extent, V111 are close to the active site and may interact with the alkyl side-chain of the substrate.

      • KCI등재

        Effect of Mutagenesis of V111 and L112 on the Substrate Specificity of Zymomonas mobilis Pyruvate Decarboxylase

        Duggleby, Ronald G.,Huang, Chang-Yi,Nixon,Peter F. The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.1

        Pyruvate decarboxylase (PDC) catalyzes the conversion of pyruvate to acetaldehyde as the penultimate step in alcohol fermentation. The enzyme requires two cofactors, thiamin diphosphate (ThDP) and Mg²+ for activity. Zymomonas PDC shows a strong preference for pyruvate although it will use the higher homologues 2-ketobutyrate and 2-ketovalerate to some extent. We have investigated the effect of mutagenesis of valine 111 and leucine 112 on the substrate specificity. V111 was replaced by glycine, alanine, leucine, and isoleucine while L112 was replaced by alanine, valine, and isoleucine. With the exception of L112I, all mutants retains activity towards pyruvate with k cat values ranging from 40% to 139% of wild-type. All mutants show changes from wild-type in the affinity for ThDP, and several (V111A, L112A, and L112V) show decreases in the affinity for Mg²+. Two of the mutants, V111G and V111A, show an increase in the K m for pyruvate. The activity of each mutant towards 2-ketobutyrate and 2-ketovalerate was investigated and some changes from wild-type were found. For the V111 mutants, the most notable of these is a 3.7-fold increase in the ability to use 2-ketovalerate. However, the largest effect is observed for the L112V mutation which increases the ability to use both 2-ketobutyrate (4.3-fold) and 2-ketovalerate (5.7-fold). The results suggest that L112 and, to a lesser extent, V111 are close to the active site and may interact with the alkyl side-chain of the substrate.

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