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Zubaidah Zubaidah - One of the best experts on this subject based on the ideXlab platform.

  • Penggunaan Bungkil Inti Sawit dan Enzim Mannanase dalam Ransum terhadap Performa Produksi Telur Puyuh (Coturnix coturnix japonica)
    'Pusat Unggulan Riset-Penggembangan Lahan Suboptimal (PUR-PLSO)', 2019
    Co-Authors: Noferdiman Noferdiman, Sestilawarti Sestilawarti, Zubaidah Zubaidah
    Abstract:

    Noferdiman et al, 2019. The use of palm kernel meal and Mannanase enzyme in diets on the production performance of quails (Coturnix coturnix japonica) . JLSO 8(1):11-19.The objective of the study was to investigate the effect of the levels of palm kernel meal and Mannanase enzyme in diets to get the best performance of quails. It was used the 180 female quails in treatment combination using the completely randomized design in factorial arrangement of 2 x 3 with 3 replications. Each unit study consisted of  10 quails. The treatment consisted of 2 levels of Mannanase enzyme, i.e. 0.00, 0.10 % and 3 levels of palm kernel meal additions, i.e. 0, 10 and 20 %. The results of the study showed that the use of Mannanase enzyme and palm kernel meal and their interaction were no significant (P>0.05) affected feed consumption, eggs production, feed conversion, egg weight, egg shell thickness, and haugh unit (HU). The use of Mannanase enzyme highly significant (P

  • Penggunaan Bungkil Inti Sawit dan Enzim Mannanase dalam Ransum terhadap Performa Produksi Telur Puyuh (Coturnix coturnix japonica)
    'Pusat Unggulan Riset-Penggembangan Lahan Suboptimal (PUR-PLSO)', 2019
    Co-Authors: Noferdiman Noferdiman, Sestilawarti Sestilawarti, Zubaidah Zubaidah
    Abstract:

    Noferdiman et al, 2019. The use of palm kernel meal and Mannanase enzyme in diets on the production performance of quails (Coturnix coturnix japonica) . JLSO 8(1):11-19.The objective of the study was to investigate the effect of the levels of palm kernel meal and Mannanase enzyme in diets to get the best performance of quails. It was used the 180 female quails in treatment combination using the completely randomized design in factorial arrangement of 2 x 3 with 3 replications. Each unit study consisted of  10 quails. The treatment consisted of 2 levels of Mannanase enzyme, i.e. 0.00, 0.10 % and 3 levels of palm kernel meal additions, i.e. 0, 10 and 20 %. The results of the study showed that the use of Mannanase enzyme and palm kernel meal and their interaction were no significant (P>0.05) affected feed consumption, eggs production, feed conversion, egg weight, egg shell thickness, and haugh unit (HU). The use of Mannanase enzyme highly significant (P<0.01) affected on eggs production and feed conversion however there were no interaction between the treatments. It was concluded that the addition of 0.10 % of Mannanase enzyme in diets consisting 20% palm kernel meal can improve the performance egg production of quails

Borun Zhang - One of the best experts on this subject based on the ideXlab platform.

  • inducible and constitutive expression of a novel thermostable alkaline β Mannanase from alkaliphilic bacillus sp n16 5 in pichia pastoris and characterization of the recombinant enzyme
    Enzyme and Microbial Technology, 2008
    Co-Authors: Nan Liu, Zhengying Zhang, Borun Zhang
    Abstract:

    Abstract A novel thermostable alkaline β-Mannanase from alkaliphilic Bacillus sp. N16-5 was expressed successfully in Pichia pastoris GS115. The combined usage of inducible and constitutive promoters ( AOX1 and GAP ) enhanced the expression of β-Mannanase. Among the parameters investigated in shaking flask cultures, the pH value of medium had significant influence on the production of β-Mannanase by recombinant P. pastoris . β-Mannanase produced at pH 7.0 was 6.7 times of that at pH value of 6.0. The highest β-Mannanase activity of 32.2 IU/ml in culture supernatant was achieved at 120 h of cultivation in BMGY medium (pH 7.0). The recombinant β-Mannanase was purified and characterized. The purified β-Mannanase produced by P. pastoris has optimum pH of 10.0 and optimum temperature of 70 °C, which are very close to those of the native enzyme from alkaliphilic Bacillus sp. N16-5. However, much higher thermal stability and pH stability were observed in recombinant β-Mannanase. These properties make the recombinant β-Mannanase more useful in the detergent industries, the pulp and paper processing and other industrial processes.

Harry J Gilbert - One of the best experts on this subject based on the ideXlab platform.

  • A β-Mannanase with a Lysozyme-like Fold and a Novel Molecular Catalytic Mechanism
    ACS central science, 2016
    Co-Authors: Yi Jin, Harry J Gilbert, Lluís Raich, Carme Rovira, M. Petricevic, Alan John, Huw T. Jenkins, Leticia Portela De Souza, Fiona Cuskin, Ethan D. Goddard-borger
    Abstract:

    The enzymatic cleavage of β-1,4-mannans is achieved by endo-β-1,4-Mannanases, enzymes involved in germination of seeds and microbial hemicellulose degradation, and which have increasing industrial and consumer product applications. β-Mannanases occur in a range of families of the CAZy sequence-based glycoside hydrolase (GH) classification scheme including families 5, 26, and 113. In this work we reveal that β-Mannanases of the newly described GH family 134 differ from other Mannanase families in both their mechanism and tertiary structure. A representative GH family 134 endo-β-1,4-Mannanase from a Streptomyces sp. displays a fold closely related to that of hen egg white lysozyme but acts with inversion of stereochemistry. A Michaelis complex with mannopentaose, and a product complex with mannotriose, reveal ligands with pyranose rings distorted in an unusual inverted chair conformation. Ab initio quantum mechanics/molecular mechanics metadynamics quantified the energetically accessible ring conformations and provided evidence in support of a 1C4 → 3H4‡ → 3S1 conformational itinerary along the reaction coordinate. This work, in concert with that on GH family 124 cellulases, reveals how the lysozyme fold can be co-opted to catalyze the hydrolysis of different polysaccharides in a mechanistically distinct manner.

  • understanding how the complex molecular architecture of mannan degrading hydrolases contributes to plant cell wall degradation
    Journal of Biological Chemistry, 2014
    Co-Authors: Harry J Gilbert, Xiaoyang Zhang, Artur Rogowski, Lei Zhao, Michael G Hahn, Utku Avci, Paul J Knox
    Abstract:

    Microbial degradation of plant cell walls is a central component of the carbon cycle and is of increasing importance in environmentally significant industries. Plant cell wall-degrading enzymes have a complex molecular architecture consisting of catalytic modules and, frequently, multiple non-catalytic carbohydrate binding modules (CBMs). It is currently unclear whether the specificities of the CBMs or the topology of the catalytic modules are the primary drivers for the specificity of these enzymes against plant cell walls. Here, we have evaluated the relationship between CBM specificity and their capacity to enhance the activity of GH5 and GH26 Mannanases and CE2 esterases against intact plant cell walls. The data show that cellulose and mannan binding CBMs have the greatest impact on the removal of mannan from tobacco and Physcomitrella cell walls, respectively. Although the action of the GH5 Mannanase was independent of the context of mannan in tobacco cell walls, a significant proportion of the polysaccharide was inaccessible to the GH26 enzyme. The recalcitrant mannan, however, was fully accessible to the GH26 Mannanase appended to a cellulose binding CBM. Although CE2 esterases display similar specificities against acetylated substrates in vitro, only CjCE2C was active against acetylated mannan in Physcomitrella. Appending a mannan binding CBM27 to CjCE2C potentiated its activity against Physcomitrella walls, whereas a xylan binding CBM reduced the capacity of esterases to deacetylate xylan in tobacco walls. This work provides insight into the biological significance for the complex array of hydrolytic enzymes expressed by plant cell wall-degrading microorganisms.

  • a family 26 Mannanase produced by clostridium thermocellum as a component of the cellulosome contains a domain which is conserved in Mannanases from anaerobic fungi
    Microbiology, 1999
    Co-Authors: Jonathan R Halstead, Harry J Gilbert, Philip E Vercoe, Keith Davidson, Geoffrey P. Hazlewood
    Abstract:

    Cellulosomes prepared by the cellulose affinity digestion method from Clostridium thermocellum culture supernatant hydrolysed carob galactomannan during incubation at 60 °C and pH 6·5. A recombinant phage expressing Mannanase activity was isolated from a library of C. thermocellum genomic DNA constructed in λZAPII. The cloned fragment of DNA containing a putative Mannanase gene (manA) was sequenced, revealing an ORF of 1767 nt, encoding a protein (Mannanase A; Man26A) of 589 aa with a molecular mass of 66816 Da. The putative catalytic domain (CD) of Man26A, identified by gene sectioning and sequence comparisons, displayed up to 32% identity with other Mannanases belonging to family 26. Immediately downstream of the CD and separated from it by a short proline/threonine linker was a duplicated 24-residue dockerin motif, which is conserved in all C. thermocellum cellulosomal enzymes described thus far and mediates their attachment to the cellulosome-integrating protein (CipA). Man26A consisting of the CD alone (Man26A′) was hyperexpressed in Escherichia coli BL21(DE3) and purified. The truncated enzyme hydrolysed soluble and insoluble mannan, displaying a temperature optimum of 65 °C and a pH optimum of 6·5, but exhibited no activity against other plant cell wall polysaccharides. Antiserum raised against Man26A′ cross-reacted with a polypeptide with a molecular mass of 70000 Da that is part of the C. thermocellum cellulosome. A second variant of Man26A containing the N-terminal segment of 130 residues and the CD (Man26A′′) bound to ivory-nut mannan and weakly to soluble Carob galactomannan and insoluble cellulose. Man26A′ consisting of the CD alone did not bind to these polysaccharides. These results indicate that the N-terminal 130 residues of mature Man26A may constitute a weak mannan-binding domain. Sequence comparisons revealed a lack of identity between this region of Man26A and other polysaccharide-binding domains, but significant identity with a region conserved in the three family 26 Mannanases from the anaerobic fungus Piromyces equi.

  • evidence that the piromyces gene family encoding endo 1 4 Mannanases arose through gene duplication
    Fems Microbiology Letters, 1996
    Co-Authors: S J Millwardsadler, Geoffrey P. Hazlewood, Gary W Black, Judith Hall, Harry J Gilbert
    Abstract:

    The sequences of two Piromyces cDNAs (manB and manC) encoding functional Mannanases, defined as Mannanase B (MANB) and Mannanase C (MANC), revealed that both the cDNAs, and the encoded enzymes, exhibited extensive sequence identity with each other and with a previously described Piromyces Mannanase. MANB and MANC, which belong to glycosyl hydrolase family 26, hydrolyse several forms of mannan but do not attack the other major plant structural polysaccharides. The data presented in this paper indicate that the Piromyces gene family encoding Mannanases arose through gene duplication.

  • the conserved noncatalytic 40 residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain
    Journal of Biological Chemistry, 1995
    Co-Authors: Cristina Fanutti, Geoffrey P. Hazlewood, Gary W Black, Tamas Ponyi, Harry J Gilbert
    Abstract:

    Abstract Two cDNAs, designated xynA and manA, encoding xylanase A (XYLA) and Mannanase A (MANA), respectively, were isolated from a cDNA library derived from mRNA extracted from the anaerobic fungus, Piromyces. XYLA and MANA displayed properties typical of endo-β1,4-xylanases and Mannanases, respectively. Neither enzyme hydrolyzed cellulosic substrates. The nucleotide sequences of xynA and manA revealed open reading frames of 1875 and 1818 base pairs, respectively, coding for proteins of M 68,049 (XYLA) and 68,055 (MANA). The deduced primary structure of MANA revealed a 458-amino acid sequence that exhibited identity with Bacillus and Pseudomonas fluorescens subsp. cellulosa Mannanases belonging to glycosyl hydrolase Family 26. A 40-residue reiterated sequence, which was homologous to duplicated noncatalytic domains previously observed in Neocallimastix patriciarum xylanase A and endoglucanase B, was located at the C terminus of MANA. XYLA contained two regions that exhibited sequence identity with the catalytic domains of glycosyl hydrolase Family 11 xylanases and were separated by a duplicated 40-residue sequence that exhibited strong homology to the C terminus of MANA. Analysis of truncated derivatives of MANA confirmed that the N-terminal 458-residue sequence constituted the catalytic domain, while the C-terminal domain was not essential for the retention of catalytic activity. Similar deletion analysis of XYLA showed that the C-terminal catalytic domain homologue exhibited catalytic activity, but the corresponding putative N-terminal catalytic domain did not function as a xylanase. Fusion of the reiterated noncatalytic 40-residue sequence conserved in XYLA and MANA to glutathione S-transferase, generated a hybrid protein that did not associate with cellulose, but bound to 97- and 116-kDa polypeptides that are components of the multienzyme cellulase-hemicellulase complexes of Piromyces and Neocallimastix patriciarum, respectively. The role of this domain in the assembly of the enzyme complex is discussed.

Lisboa, César Gustavo Serafim - One of the best experts on this subject based on the ideXlab platform.

  • Endo-beta-mananase de endosperma de Sesbania virgata (Cv.) Pers. : purificação, caracterização e importancia na germinação e desenvolvimento da plantula
    [s.n.], 2018
    Co-Authors: Lisboa, César Gustavo Serafim
    Abstract:

    Orientador: Marcos Silveira BuckeridgeDissertação (mestrado) - Universidade Estadual de Campinas, Instituto de BiologiaResumo: As sementes de muitas plantas possuem endosperma, um tecido especializado com funções tanto de reserva como de constrição mecânica do embrião nas primeiras etapas de desenvolvimento. Em muitas espécies de leguminosas, estes tecidos especializados armazenam como polissacarídeo de reserva, o galactomanano. Este polímero apresenta um cadeia central de manose ( ß-1,4 ligadas) e ramificações de galactose (?-l,6 ligadas ao esqueleto central). Três enzimas estão envolvidas na hidrólise do galactomanano: a endo-ß- mananase, a ?-galactosidase e a ß-manosidase. Da forma com que a endo-mananase ataca o polímero, inicialmente produz oligossacarídeos galactosilados que, são posteriormente hidrolisados pelas duas últimas exo-enzimas (?-galactosidase e ß-mananase) até galactose e manose livres. Neste trabalho, uma endo-ß-mananase foi purificada do endosperma das sementes de Sesbania virgata, uma leguminosa nativa. Uma curva de tempo de germinação mostrou que a atividade da mananase aparece inicialmente na região do endosperma próxima à área de protrusão da radícula e, subseqüentemente, aumenta na região lateral do endosperma da semente seguindo o desenvolvimento da plântula. Medindo a atividade em pH 5 a 45°C, o máximo da atividade catalítica correspondeu a 120h de desenvolvimento para, em seguida, decair. Para a purificação da enzima, utilizou-se uma coluna de troca iônica DEAE-celulose seguida de uma coluna de afinidade biológica em Sepharose Concanavalina A. A mananase purificada é uma glicoproteína de peso molecular de cerca de 30KDa, com pH ótimo entre 3,5 e 5, temperatura ótima de 45°C e ponto isoelétrico 4,5. A caracterização da atividade da endo-mananase sobre diferentes galactomananos com diferentes razões manose:galactose, indicou que a ramificação do polissacarídeo com galactose é o "fator-chave" na modulação da própria ação catalítica dessa enzima. Com essas observações, foi concluído que, a atividade da endo-mananase, além de estar relacionada com a mobilização de reservas, facilita a emersão da radícula agindo na área próxima à protrusão. Entendendo que a mananase pura não foi capaz de degradar o galactomanano da Trigonellafoenum-graecum (razão 1:1 de manose/galactose), sugere-se que exista uma relação inversa entre o grau de ramificação e a porcentagem de hidrólise da endo-mananaseAbstract; Many plant seeds have an endosperm, a tissue specialised either as storage or mechanical constraint to embryo growth. In many legume species, endosperms contain galactomannan. This polyssacharide is composed of a main chain of 1,4-ß-mannan branched with variable amounts of 1,6-?-linked galactosyl residues. Three enzymes produced by an aleurone layer are involved in galactomannan hydrolysis: endo-ß-Mannanase, ?-galactosidase and ß- mannosidase. The former with Mannanase attacks the polymer producing galactosylated oligossacharides which are further hydrolysed by the two last exo-enzymes to free mannose and galactose. In the present work, an endo-ß-Mannanase was purified from the endosp erm of Sesbanía vírgata, a Brazilian native legume. The time-course shows that the activity of Mannanase appears initially in the endosperm cap of seeds prior to radicle emergence and subsequently increases in the remaining lateral endosperm following seedling growth. Measuring the activity at pH 5 and 45°C, endo-Mannanase peaked at 120h and then decreased. We used these conditions to perform purification procedures in DEAE-cellulose followed by affinity chromatography with Sepharose Concanavaline-A. The enzyme is a glycoprotein with an apparent molecular weight of 30Kda, optimum pH at 4.5 and temperature at 45°C, pI at 4.5. The mode of action of the enzyme on different galactomannans indicates the modulation of Mannanase activity by the branching pattems of the polymers with galactose. From these observations it was concluded that Mannanase activity facilitates radicle protrusion through the surrounding endosperm by weakening it in the area close to the radicle tip. On the basis that the pure enzyme can not degrade the fenugreek galactomannan (a fully substituted polysaccharide), we suggest that there is an inverse relationship between galactose branching and the degree of hydrolysisMestradoBiologia CelularMestre em Biologia Celular e Estrutura

  • Endo-beta-mananase do endosperma de sementes de Sesbania virgata (Cav.) Pers. (Leguminosae): purificação, caracterização e seu duplo papel na germinação e crescimento inicial da plântula
    Brazilian Journal of Plant Physiology, 2015
    Co-Authors: Lisboa, César Gustavo Serafim, Tonini, Patrícia Pinho, Tiné, Marco Aurélio Silva, Buckeridge, Marcos Silveira
    Abstract:

    Galactomannans are storage cell wall polysaccharides present in seeds of some legumes. Their degradation is carried out by three hydrolases (alpha-galactosidase (EC 3.2.1.22), endo-beta-Mannanase (EC 3.2.1.78) and ß-mannosidase (EC 3.2.1.25)). In the present study we purified and characterised an endo-beta-Mannanase from seeds of Sesbania virgata and addressed its role in germination and seedling development. The polypeptide purified by Ion Exchange Chromatography and Affinity Chromatography on Sepharose-Concanavalin A, showed a pH optimum between 3.5 and 5 at 45ºC and high stability at pH 7.8. The low stability at pH 5 appears to be associated with isoelectric precipitation, in view of the pI of the enzyme being 4.5. The purified enzyme is a glycoprotein with a molecular mass of 26 KDa by SDS-PAGE and 36 KDa by gel chromatography. The purified polypeptide attacked galactomannan from different sources, being more effective on polymers with a lower degree of galactosylation (from carob gum), in comparison with medium or highly galactosylated galactomannans (from guar, S. virgata and fenugreek), respectively. A peak of endo-beta-Mannanase activity was detected during radicle protrusion in the endosperm tissue surrounding the radicle and later on in the lateral endosperm. This second peak was associated with the period of reserve mobilisation. Using an antibody raised against coffee endo-beta-Mannanase, the enzyme could be detected in immunodot-blots performed with extracts of S. virgata endosperms. The results are consistent with the hypothesis that the peak of endo-Mannanase during germination facilitates radicle protrusion through the surrounding endosperm by weakening it in the region close to the radicle tip.Galactomananos são polissacarídeos de reserva de parede celular presentes em sementes de leguminosas. Sua degradação é efetuada por três hidrolases (alfa-galactosidase (EC 3.2.1.22), endo-beta-mananase (EC 3.2.1.78) e manosidase (EC 3.2.1.25)). No presente estudo, nós purificamos e caracterizamos uma endo-beta-mananase de sementes de Sesbania virgata e focamos no seu papel na germinação e no desenvolvimento da plântula. A enzima foi purificada por cromatografia de troca iônica e cromatografia de afinidade em sepharose-concanavalina A, mostrando um pH ótimo entre 3,5 e 5 a 45 ºC e alta estabilidade em pH 7,8. A baixa estabilidade em pH 5 parece estar associada à precipitação isoelétrica, pois o pI da enzima é 4,5. O polipeptídeo purificado é uma glicoproteína com massa molecular de 26 KDa em SDS-PAGE e 36 KDa em cromatografia em gel. O polipeptídeo purificado atacou galactomamano de diferentes fontes, sendo efetivo sobre polímeros com grau de galactosilação mais baixo (goma caroba), em comparação com galactomamanos com médio e alto graus de galactosilação (guar, S. virgata e feno grego), respectivamente. Um pico de atividade de endo-beta-mananase foi detectado durante a protrusão da radícula no tecido endospérmico ao redor da radícula e mais tarde nas porções laterais do endosperma. O segundo pico foi inversamente associado à mobilização de reservas. Usando um anticorpo feito contra endo-beta-mananase de café, a enzima foi detectada por immunodot-blots feitos com extratos de endosperma de S. virgata. Os resultados são consistentes com a hipótese de que o pico de endo-mananase durante a germinação facilita a protrusão da radícula através do enfraquecimento do endosperma que circunda a área próxima à ponta da radícula

  • Endo-beta-mananase do endosperma de sementes de Sesbania virgata (Cav.) Pers. (Leguminosae): purificação, caracterização e seu duplo papel na germinação e crescimento inicial da plântula
    Brazilian Journal of Plant Physiology, 2015
    Co-Authors: Lisboa, César Gustavo Serafim, Tonini, Patrícia Pinho, Tiné, Marco Aurélio Silva, Buckeridge, Marcos Silveira
    Abstract:

    Galactomannans are storage cell wall polysaccharides present in seeds of some legumes. Their degradation is carried out by three hydrolases (alpha-galactosidase (EC 3.2.1.22), endo-beta-Mannanase (EC 3.2.1.78) and ß-mannosidase (EC 3.2.1.25)). In the present study we purified and characterised an endo-beta-Mannanase from seeds of Sesbania virgata and addressed its role in germination and seedling development. The polypeptide purified by Ion Exchange Chromatography and Affinity Chromatography on Sepharose-Concanavalin A, showed a pH optimum between 3.5 and 5 at 45ºC and high stability at pH 7.8. The low stability at pH 5 appears to be associated with isoelectric precipitation, in view of the pI of the enzyme being 4.5. The purified enzyme is a glycoprotein with a molecular mass of 26 KDa by SDS-PAGE and 36 KDa by gel chromatography. The purified polypeptide attacked galactomannan from different sources, being more effective on polymers with a lower degree of galactosylation (from carob gum), in comparison with medium or highly galactosylated galactomannans (from guar, S. virgata and fenugreek), respectively. A peak of endo-beta-Mannanase activity was detected during radicle protrusion in the endosperm tissue surrounding the radicle and later on in the lateral endosperm. This second peak was associated with the period of reserve mobilisation. Using an antibody raised against coffee endo-beta-Mannanase, the enzyme could be detected in immunodot-blots performed with extracts of S. virgata endosperms. The results are consistent with the hypothesis that the peak of endo-Mannanase during germination facilitates radicle protrusion through the surrounding endosperm by weakening it in the region close to the radicle tip.Galactomananos são polissacarídeos de reserva de parede celular presentes em sementes de leguminosas. Sua degradação é efetuada por três hidrolases (alfa-galactosidase (EC 3.2.1.22), endo-beta-mananase (EC 3.2.1.78) e manosidase (EC 3.2.1.25)). No presente estudo, nós purificamos e caracterizamos uma endo-beta-mananase de sementes de Sesbania virgata e focamos no seu papel na germinação e no desenvolvimento da plântula. A enzima foi purificada por cromatografia de troca iônica e cromatografia de afinidade em sepharose-concanavalina A, mostrando um pH ótimo entre 3,5 e 5 a 45 ºC e alta estabilidade em pH 7,8. A baixa estabilidade em pH 5 parece estar associada à precipitação isoelétrica, pois o pI da enzima é 4,5. O polipeptídeo purificado é uma glicoproteína com massa molecular de 26 KDa em SDS-PAGE e 36 KDa em cromatografia em gel. O polipeptídeo purificado atacou galactomamano de diferentes fontes, sendo efetivo sobre polímeros com grau de galactosilação mais baixo (goma caroba), em comparação com galactomamanos com médio e alto graus de galactosilação (guar, S. virgata e feno grego), respectivamente. Um pico de atividade de endo-beta-mananase foi detectado durante a protrusão da radícula no tecido endospérmico ao redor da radícula e mais tarde nas porções laterais do endosperma. O segundo pico foi inversamente associado à mobilização de reservas. Usando um anticorpo feito contra endo-beta-mananase de café, a enzima foi detectada por immunodot-blots feitos com extratos de endosperma de S. virgata. Os resultados são consistentes com a hipótese de que o pico de endo-mananase durante a germinação facilita a protrusão da radícula através do enfraquecimento do endosperma que circunda a área próxima à ponta da radícula.269280Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq

Noferdiman Noferdiman - One of the best experts on this subject based on the ideXlab platform.

  • Penggunaan Bungkil Inti Sawit dan Enzim Mannanase dalam Ransum terhadap Performa Produksi Telur Puyuh (Coturnix coturnix japonica)
    'Pusat Unggulan Riset-Penggembangan Lahan Suboptimal (PUR-PLSO)', 2019
    Co-Authors: Noferdiman Noferdiman, Sestilawarti Sestilawarti, Zubaidah Zubaidah
    Abstract:

    Noferdiman et al, 2019. The use of palm kernel meal and Mannanase enzyme in diets on the production performance of quails (Coturnix coturnix japonica) . JLSO 8(1):11-19.The objective of the study was to investigate the effect of the levels of palm kernel meal and Mannanase enzyme in diets to get the best performance of quails. It was used the 180 female quails in treatment combination using the completely randomized design in factorial arrangement of 2 x 3 with 3 replications. Each unit study consisted of  10 quails. The treatment consisted of 2 levels of Mannanase enzyme, i.e. 0.00, 0.10 % and 3 levels of palm kernel meal additions, i.e. 0, 10 and 20 %. The results of the study showed that the use of Mannanase enzyme and palm kernel meal and their interaction were no significant (P>0.05) affected feed consumption, eggs production, feed conversion, egg weight, egg shell thickness, and haugh unit (HU). The use of Mannanase enzyme highly significant (P

  • Penggunaan Bungkil Inti Sawit dan Enzim Mannanase dalam Ransum terhadap Performa Produksi Telur Puyuh (Coturnix coturnix japonica)
    'Pusat Unggulan Riset-Penggembangan Lahan Suboptimal (PUR-PLSO)', 2019
    Co-Authors: Noferdiman Noferdiman, Sestilawarti Sestilawarti, Zubaidah Zubaidah
    Abstract:

    Noferdiman et al, 2019. The use of palm kernel meal and Mannanase enzyme in diets on the production performance of quails (Coturnix coturnix japonica) . JLSO 8(1):11-19.The objective of the study was to investigate the effect of the levels of palm kernel meal and Mannanase enzyme in diets to get the best performance of quails. It was used the 180 female quails in treatment combination using the completely randomized design in factorial arrangement of 2 x 3 with 3 replications. Each unit study consisted of  10 quails. The treatment consisted of 2 levels of Mannanase enzyme, i.e. 0.00, 0.10 % and 3 levels of palm kernel meal additions, i.e. 0, 10 and 20 %. The results of the study showed that the use of Mannanase enzyme and palm kernel meal and their interaction were no significant (P>0.05) affected feed consumption, eggs production, feed conversion, egg weight, egg shell thickness, and haugh unit (HU). The use of Mannanase enzyme highly significant (P<0.01) affected on eggs production and feed conversion however there were no interaction between the treatments. It was concluded that the addition of 0.10 % of Mannanase enzyme in diets consisting 20% palm kernel meal can improve the performance egg production of quails