Evaluation of Different Yeast Species for Improving In vitro Fermentation of Cereal Straws

Wang, Zuo,He, Zhixiong,Beauchemin, Karen A.,Tang, Shaoxun,Zhou, Chuanshe,Han, Xuefeng,Wang, Min,Kang, Jinhe,Odongo, Nicholas E.,Tan, Zhiliang Asian Australasian Association of Animal Productio 2016 Animal Bioscience Vol.29 No.2

Information on the effects of different yeast species on ruminal fermentation is limited. This experiment was conducted in a $3{\times}4$ factorial arrangement to explore and compare the effects of addition of three different live yeast species (Candida utilis 1314, Saccharomyces cerevisiae 1355, and Candida tropicalis 1254) at four doses (0, $0.25{\times}10^7$, $0.50{\times}10^7$, and $0.75{\times}10^7$ colony-forming unit [cfu]) on in vitro gas production kinetics, fiber degradation, methane production and ruminal fermentation characteristics of maize stover, and rice straw by mixed rumen microorganisms in dairy cows. The maximum gas production (Vf), dry matter disappearance (IVDMD), neutral detergent fiber disappearance (IVNDFD), and methane production in C. utilis group were less (p<0.01) than other two live yeast supplemented groups. The inclusion of S. cerevisiae reduced (p<0.01) the concentrations of ammonia nitrogen ($NH_3$-N), isobutyrate, and isovalerate compared to the other two yeast groups. C. tropicalis addition generally enhanced (p<0.05) IVDMD and IVNDFD. The $NH_3$-N concentration and $CH_4$ production were increased (p<0.05) by the addition of S. cerevisiae and C. tropicalis compared with the control. Supplementation of three yeast species decreased (p<0.05) or numerically decreased the ratio of acetate to propionate. The current results indicate that C. tropicalis is more preferred as yeast culture supplements, and its optimal dose should be $0.25{\times}10^7$ cfu/500 mg substrates in vitro.

Molecular Cloning, Tissue Distribution and Segmental Ontogenetic Regulation of b^0,+ Amino Acid Transporter in Lantang Pigs

Zhi, Ai-Min,Feng, Ding-Yuan,Zhou, Xiang-Yan,Zou, Shi-Geng,Huang, Zhi-Yi,Zuo, Jian-Jun,Ye, Hui,Zhang, Chang-Ming,Dong, Ze-Min,Liu, Zhun Asian Australasian Association of Animal Productio 2008 Animal Bioscience Vol.21 No.8

Cationic amino acid transporter $b^{0,+}AT$ (HGMW-approved gene symbol SLC7A9, solute carrier family 7, member 9) plays a crucial role in amino acid nutrition. In the present study, we describe the cloning and sequencing of porcine $b^{0,+}AT$. Based on the sequence of porcine $b^{0,+}AT$ deposited in the NCBI (National Center for Biotechnological Information), we identified a putative porcine homologue. Using rapid amplification of cDNA ends (RACE), the full-length cDNA encoding porcine $b^{0,+}AT$ was isolated. The porcine $b^{0,+}AT$ cDNA was 1,680 bp long, encoding a 487 amino acid trans-membrane protein. The predicted amino acid sequence was found to have 88.9% and 87.1% identity with human and mouse $b^{0,+}AT$, respectively. Real-time RT-PCR indicated porcine $b^{0,+}AT$ transcripts expressed in heart, kidney, muscle and small intestine. The small intestine had the highest $b^{0,+}AT$ mRNA abundance while the muscle had the lowest (p<0.05). Along the longitudinal axis, the ileum had the highest $b^{0,+}AT$ mRNA abundance while the colon had the lowest (p<0.05). The $b^{0,+}AT$ mRNA level was highest on day 7 and 90 in the duodenum (p<0.05). It increased from day 1 to day 26 in the jejunum (p>0.05) and had the highest abundance on day 60 (p<0.05). There was, however, no difference between day 1, 7, 26, 30, 90 and 150 (p>0.05). The strongest $b^{0,+}AT$ expression appeared on day 7 in the ileum before weaning, and then decreased till day 30 but rose gradually again from day 60 to 150 (p<0.05).

Molecular Cloning, Tissue Distribution and Expression of Porcine y⁺L Amino Acid Transporter-1

Zhi, Ai-min,Zhou, Xiang-yan,Zuo, Jian-jun,Zou, Shi-geng,Huang, Zhi-yi,Wang, Xiao-lan,Tao, Lin,Feng, Ding-yuan Asian Australasian Association of Animal Productio 2010 Animal Bioscience Vol.23 No.2

In this study, we cloned, sequenced and characterized porcine y+L Amino Acid Transporter-1 (y+LAT1). By screening a translated EST database with the protein sequence of the human $y^{+}$LAT1 and by using rapid amplification of cDNA ends (RACE), the full-length cDNA encoding porcine $y^{+}$LAT1 was isolated from porcine intestine RNA. It was 2,111 bp long, encoding a 511 amino acid trans-membrane glycoprotein composed of 12 transmembrane domains. The predicted amino acid sequence was found to be 91%, 90%, 87% and 87% identical to those of cattle, human, mouse and rat $y^{+}$LAT1 respectively. Real-time RT-PCR results indicated that the small intestine had the highest $y^{+}$LAT1 mRNA abundance and the lung had the lowest $y^{+}$LAT1 mRNA abundance. Baby hamster kidney (BHK) cells transfected with green fluorescent protein (GFP) tagged porcine $y^{+}$LAT1 cDNA indicated that the cellular localization of the gene product in BHK was on the plasma membrane.

Optimized Assembly of Micro-/Meso-/Macroporous Carbon for Li–S Batteries

Qiong Tang,Heqin Li,Min Zuo,Jing Zhang,Yiqin Huang,Peiwen Bai,Jiaqi Xu,Kuan Zhou 성균관대학교(자연과학캠퍼스) 성균나노과학기술원 2017 NANO Vol.12 No.2

In order to explore the effect of hierarchical porous carbon on the performances of Li–S batteries, we synthesized three kinds of micro-/meso-/macroporous carbon materials with different pore properties by facile hard-template method. Different from the majority of reports on porous carbon ensuing large specific surface area (SSA) and total pore volume, it was found that in the case of identically high sulfur content, the pore size distribution substantially influences the performances of Li–S batteries rather than the SSA and total pore volume. Furthermore, in the assembly of micro-/meso-/macropores, the micropore volume ratio to the total pore volume is dominant to the capabilities of batteries. Among the samples, the porous carbon carbonized with the precursor of sucrose at 950℃ presents the highest initial discharge specific capacity of 1327 mAh/g and retention of 630 mAh/g over 100 cycles at 0.2C rate along with the best rate capability. This sample possesses the largest micropore volume ratio of 47.54% but a medium SSA of 1217 m2 /g and inferior total pore volume of 0.54 cm3 /g. The abundant micropores effectively improve the conductivity of dispersed sulfur particles, inhibit the loss of sulfur series and enable the cathode to exhibit superior electrochemical performances.

Restoration of NAD + homeostasis protects C2C12 myoblasts and mouse levator ani muscle from mechanical stress-induced damage

Guotao Huang,Yong He,Li Hong,Min Zhou,Xiaohu Zuo,Zhihan Zhao 한국통합생물학회 2022 Animal cells and systems Vol.26 No.4

Excessive mechanical traction damages the levator ani muscle (LAM), increasing the incidence of pelvic floor dysfunction (PFD). In this study, we explored the effects of oxidized nicotinamide adenine dinucleotide (NAD+) on the damage to both muscle cells and LAM tissue induced by mechanical stress (MS) at the cellular and animal levels. The cell damage model was established using a four-point bending system. The LAM damage model was established using vaginal distention and traction. Exogenous addition of PJ34, an inhibitor of poly (ADP-ribose) polymerase-1 (PARP-1), and the nicotinamide mononucleotide (NMN) precursor of NAD+ increased NAD+ levels. ATP content and mitochondrial membrane potential were measured to assess mitochondrial function. NAD+ levels, cell viability, and PARP-1 activity were detected using commercial kits. DNA damage in cells was detected with immunofluorescence staining, and LAM damage was detected with tissue TUNEL staining. PARP-1 activity and DNA damage of LAM were detected by immunohistochemistry. A small amount of DNA damage and PARP-1 activation did not affect NAD+ levels, while excessive DNA damage and PARP-1 activation led to an imbalance of NAD+ homeostasis. Furthermore, increasing NAD+ levels in vivo and in vitro could rescue mitochondrial dysfunction and damage to both muscle cells and LAM tissue induced by MS. In conclusion, MS can induce damage to both C2C12 cells and LAM tissue. Restoring NAD+ homeostasis can rescue this damage by improving mitochondrial function.

Molecular Cloning, Segmental Distribution and Ontogenetic Regulation of Cationic Amino Acid Transporter 2 in Pigs

Zou, Shi-geng,Zhi, Ai-min,Zhou, Xiang-yan,Zuo, Jian-jun,Zhang, Yan,Huang, Zhi-yi,Xu, Ping-Wen,Feng, Ding-yuan Asian Australasian Association of Animal Productio 2009 Animal Bioscience Vol.22 No.5

The goal of this study was to elucidate the expression and segmental distribution of the glomerular cationic amino acid metabolism transporter-2 (CAT-2) and thus to improve our understanding of porcine cationic amino acid transporters and amino acid absorption. Porcine CAT-2 was cloned, sequenced and characterized. The predicted amino acid sequence of porcine CAT-2 shared 86.1% and 92.1% identity with human and mouse CAT-2A, respectively. The tissue distribution patterns and ontogenic changes of CAT-2 mRNAs were determined by real-time Q-PCR. The results showed that porcine CAT-2 was highly expressed in the heart and intestinal tract (duodenum, ileum and jejunum). In addition, the mRNA of CAT-2 was found in liver, lung, kidney, brain and muscle. Within the intestinal tract, CAT-2 mRNA was most abundant in the ileum and rarely expressed in the duodenum. In the duodenum, the levels of CAT-2 mRNA reached their peak on day 7 (p<0.05) while in the jejunum, levels were low on day 1 and 7 and increased rapidly after day 26 before peaking on days 30 and 60 (p<0.05). The levels then dramatically decreased by day 90 (p<0.05). In the ileum, levels achieved their maximum on day 30 and then decreased significantly on day 60 (p<0.05).

Molecular Cloning, Identification and Characteristics of a Novel Isoform of Carbamyl Phosphate Synthetase 1 in Human Testis

( Ran Huo ),( Hui Zhu ),( Li Lu ),( Lan Lan Ying ),( Min Xu ),( Zhi Yang Xu ),( Jian Min Li ),( Zuo Min Zhou ),( Jia Hao Sha ) 생화학분자생물학회 2005 BMB Reports Vol.38 No.1

A gene coding a novel isoform of carbamyl phosphate synthetase I (CPSI) was cloned from a human testicular library. As shown by cDNA microarray hybridization, this gene was expressed at a higher level in human adult testes than in fetal testes. The full length of its cDNA was 3831 bp, with a 3149 bp open reading frame, encoding a 1050-amino-acid protein. The cDNA sequence was deposited in the GenBank (AY317138). Sequence analysis showed that it was homologous to the human CPS1 gene. The putative protein contained functional domains composing the intact large subunit of carbamoyl phosphate synthetase, thus indicated it has the capability of arginine biosynthesis. A multiple tissue expression profile showed high expression of this gene in human testis, suggesting the novel alternative splicing form of CPS1 may be correlated with human spermatogenesis.