CN106223096B - A method of utilizing gluing object in high temperature esterase removal secondary stock - Google Patents

A method of utilizing gluing object in high temperature esterase removal secondary stock Download PDF

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CN106223096B
CN106223096B CN201610594944.5A CN201610594944A CN106223096B CN 106223096 B CN106223096 B CN 106223096B CN 201610594944 A CN201610594944 A CN 201610594944A CN 106223096 B CN106223096 B CN 106223096B
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esterase
est1
gluing object
secondary stock
high temperature
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CN106223096A (en
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王永华
蓝东明
张泽栋
杨博
周鹏飞
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South China University of Technology SCUT
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    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21CPRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/005Treatment of cellulose-containing material with microorganisms or enzymes
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/16Hydrolases (3) acting on ester bonds (3.1)
    • C12N9/18Carboxylic ester hydrolases (3.1.1)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y301/00Hydrolases acting on ester bonds (3.1)
    • C12Y301/01Carboxylic ester hydrolases (3.1.1)
    • DTEXTILES; PAPER
    • D21PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21CPRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/02Working-up waste paper
    • YGENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02WCLIMATE CHANGE MITIGATION TECHNOLOGIES RELATED TO WASTEWATER TREATMENT OR WASTE MANAGEMENT
    • Y02W30/00Technologies for solid waste management
    • Y02W30/50Reuse, recycling or recovery technologies
    • Y02W30/64Paper recycling

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Health & Medical Sciences (AREA)
  • Wood Science & Technology (AREA)
  • Zoology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Engineering & Computer Science (AREA)
  • Genetics & Genomics (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • General Engineering & Computer Science (AREA)
  • Microbiology (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Biomedical Technology (AREA)
  • Biotechnology (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Paper (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

The invention discloses a kind of methods using gluing object in high temperature esterase removal secondary stock, and the esterase is esterase EstE1, the PDB ID:2C7B from macro genomic library.Specifically comprise the following steps: the esterase that 0.1U~1.0U/g (relative to oven dry stock quality) is added into secondary stock, handles 45~120min of time, 40~80 DEG C of temperature, pH is 5.0~9.0,100~150rpm of mixing speed.Gluing object content in secondary stock is finally detected according to TAPPIT-277 standard law.As a result confirm that stickies removal rate reaches 54.1%~66.5%, still has preferable removal effect even in a high temperature environment.The present invention carries out efficient degradation to the gluing object in secondary stock using high temperature esterase EST1, and operating process is easy and is not necessarily to additional machinery equipment, and stickies removal effect is obvious, and production cost is low, pollution-free.

Description

A method of utilizing gluing object in high temperature esterase removal secondary stock
Technical field
The present invention relates to a kind of methods using gluing object in high temperature esterase removal secondary stock.
Background technique
In recent years, secondary stock in global pulp total quantity consumed accounting more than 60%.Waste paper is as China's pulping and paper-making A kind of important source material of industry, the recycling of waste paper can not only save a large amount of plant fiber materials, reduce production cost, but also For realizing that energy-saving, alleviation environmental pollution has profound significance.However the formation of gluing object and control problem are in reality Waste paper recycle during it is increasingly prominent, gluing object refer to that various sources are different during waste paper recycling and it is permanent to have or The interim stickiness of person and all substances that problem can be caused in the paper making process and product quality is caused to decline.Gluing object main source Hot-melt object, pressure-sensitive object, sizing agent, coating gluing object and ink residue etc. in waste paper, these substances are mainly by polypropylene Acid esters, polyvinyl acetate etc. are mixed with other impurities, they are connected the basic structure component of gluing object by ester bond Together.Since elecrtonegativity is presented in gluing object in slurry system, thus various cationic substances can be adsorbed, therefore in slurrying Be easy for resulting in blockage in paper-making process mesh, there is paper cavity, generate anionic trash, disconnected paper and paper machine is caused to be shut down The problems such as.
Currently, the method for gluing object mainly uses Mechanical Method and chemical method in removal and control slurry.Mechanical Method includes sieve The physical methods such as choosing, purification, washing, flotation and heat partition are mainly used to remove the big gluing object in secondary stock.Chemical rule By adding stickies control machine, microstickies are removed using the methods of chemisorption, modification, dispersion, surface passivation.This A little methods are the common stickies control method of regenerated papermaking enterprise, although there is certain removal effect, there are highly energy-consuming, Low efficiency is also easy to produce the problems such as a large amount of industrial wastewaters, and removal efficiency will also be by factors such as the superiority and inferiority of equipment performance It influences.
Biological enzyme has efficient, single-minded, stable catalytic, and no pollution to the environment, therefore in pulping and paper-making field Using receive more and more attention, many enterprises utilize the gluing in biological enzyme processing waste paper removal process in recent years Object problem.With the development of enzyme engineering technology, the catalytic efficiency of biological enzyme, substrate specificity and stability can be mentioned further Height is particularly suited for actual production.Biological enzyme formulation currently used for paper industry has protease, cellulase, pectase, wood Dextranase, lipase and esterase etc..Wherein lipase and esterase are a kind of carboxylic ester hydrolases, have and accelerate emplastic ester bond Fracture, make its stick object product become smaller and stick efficiency decrease characteristic, can be used for controlling and removing the gluing object in waste paper. Once being broken, the basic component of gluing object is difficult to regroup in systems ester bond, and biological enzyme can voluntarily degrade, will not Pollute environment.Wan Jinquan etc. [ten thousand Jin Quan etc., gluing object biological enzyme is handled in de inked pulp] is using lipase to de inked pulp Middle gluing object is handled, and it is different to find different types of lipase treatment effect, but be difficult reality under common Pulping conditions Now preferable treatment effect.Soughing of the wind in forest trees etc. [soughing of the wind in forest trees etc., application of the stickies control enzyme in Waste Paper Handling] utilizes biological enzyme Optimyze525 handles waste paper gluing object, and stickies removal rate reaches 29.9%.
Although common lipase and esterase has certain stickies removal effect, secondary stock ingredient is complex, Containing the chemical substance that biological enzyme can largely inactivated, and the extreme environments such as high temperature easily lead to biological enzyme formulation in actual production The efficiency of application is suppressed.
Summary of the invention
For highly energy-consuming, low efficiency in existing waste paper stickies removal technique, it is also easy to produce a large amount of industrial wastewaters and general Logical biological enzyme in the high temperature environment easy in inactivation the problems such as.The present invention provides gluing object in a kind of high temperature esterase EST1 removal secondary stock Method, simple process provided by the invention, effect are obvious, easily operated.
To achieve the above object, technical solution is as follows by the present invention:
A method of using gluing object in high temperature esterase removal secondary stock, the esterase is high temperature esterase EST1, is come Derived from esterase EstE1, the PDB ID:2C7B_B of macro genomic library.Include the following steps:
(1) preparation of high temperature esterase EST1:
Esterase EST1 strain is inoculated into seed fluid nutrient mediums of saccharomycete shaken cultivation, then strain is inoculated into fermentation medium vibration Culture is swung, high temperature esterase EST1 crude enzyme liquid is prepared, high temperature esterase EST1 crude enzyme liquid is purified, with p-nitrophenol colorimetric method Measure the enzyme activity of high temperature esterase EST1.
(2) secondary stock is handled using high temperature esterase EST1:
The esterase EST1 of addition 0.1U~1.0U/g (relative to oven dry stock quality) into secondary stock, the processing time 45~ 120min, 40~80 DEG C of temperature, pH 5.0~9.0,100~150rpm of mixing speed.
(3) gluing object content in secondary stock is detected by TAPPIT-277 standard law:
Slurry is sieved using Pulmac-MasterScreen pulp classifier according to TAPPIT-277 gluing object measuring method Choosing, will sift out later gluing object dyed, tabletting, finally carry out analysis scanning with scanning software, and then measure gluing object and contain Amount.
Preferably, the esterase EST1 additive amount is 0.3~0.8U/g (relative to oven dry stock quality).
It is further preferable that the additive amount of the esterase is 0.5U/g (relative to oven dry stock).
Preferably, the temperature is 40~60 DEG C.
Preferably, the pH is 7.0~8.0.
It is further preferable that the temperature is 55 DEG C.
Preferably, the processing time is 60min.
Preferably, the mixing speed is 120rpm.
Preferably, the enzyme activity of the esterase is 125.0U/ml.
Preferably, it is 4%~6% that the slurry of the secondary stock is dense.
Compared with prior art, the beneficial effects of the present invention are:
(1) the high temperature esterase EST1 preparation in the present invention is easy, and can effectively be hydrolyzed polyacrylate in waste paper gluing object, be gathered The ingredients such as vinylacetate;It is obvious to remove waste paper gluing object effect, as a result confirm stickies removal rate reach 54.1%~ 66.5%, still there is preferable removal effect even in a high temperature environment.
(2) it is 55 DEG C that the high temperature esterase EST1 in the present invention, which is most suitable for reaction temperature, and is lived in 80 DEG C of heat preservation catalysis in 2 hours Power remains unchanged, which shows good catalytic performance and structural stability, can cope with each in waste paper recovery process Kind high temperature and acid or alkali environment, are still able to maintain preferable stickies removal effect under the high temperature conditions.
(3) present invention is directly carried out in the production line by the method that high temperature esterase EST1 removes waste paper gluing object, without Increase any mechanical equipment, it is easy to operate, it is at low cost, it is pollution-free, it efficiently, steadily solves over tight in regenerated papermaking field Ghost image rings product quality gluing object problem.
Specific embodiment
Introduce implementation of the invention in more detail by embodiment.In the described embodiment, the enzyme concentration is relative to exhausted Dry pulp Mass Calculation, experimental result, which is repeated three times, to be averaged.Esterase used in the present invention, protein sequence number is by egg White matter warehouse publication (http://www.rcsb.org/pdb/home/home.do);From the esterase of macro genomic library (EstE1, PDB ID:2C7B), amino acid sequence is as shown in SEQ ID NO:1, nucleotide sequence such as SEQ ID NO:2 institute Show.
The preparation process of esterase EST1: it using the encoding gene for the EST1 esterase that full genome synthetic method obtains, and clones Recombinant expression carrier is obtained on to expression vector pET23a-CBD carrier.Utilize CaCl2Conversion method will be encoded containing EST1 esterase The expression plasmid of gene is transferred in BL21 (DE3) strain, obtains genetic engineering bacterium.The strain of esterase EST1 is connected to containing Amp Expand culture in the LB seed culture medium of (100ug/ml), when OD value reaches 0.6~0.8, by bacterium solution according to the ratio of 1:100 It is inoculated into the LB fermentation medium containing Amp (100ug/ml), shakes to OD value and IPTG (20mmol/L) is added when being 0.6~0.8 Inducer progress inducing expression, 18~receive bacterium afterwards for 24 hours.Tube wall is collected after bacterium solution is centrifuged 10min under the conditions of 12000r/min Cell carries out ultrasonication, arrives crude enzyme liquid again later to take supernatant after 12000r/min pelleted by centrifugation 10min.It is existing Research report is specifically bound using cellulose and esterase, carries out digestion with HRV 3CP again later to obtain pure enzyme. 1L bacterium solution corresponds to 1g cellulose, 30min, in due course stirring in conjunction with cellulose by crude enzyme liquid under room temperature.In conjunction with rear high speed centrifugation 10min discards supernatant liquid, and adhesion protein is washed twice with PBS buffer solution.HRV 3CP is first being centrifuged before, is discarding supernatant, It is cleaned 2 times using PBS buffer solution.Appropriate PBS is added into adhesion protein, the ratio for corresponding to 1ml HRV 3CP in 1L bacterium solution is mixed Even rear digestion 4h is stayed overnight.High speed centrifugation after digestion, supernatant are pure enzyme.P-nitrophenol colorimetric method for determining system is utilized later The enzyme activity of standby high temperature esterase EST1, measuring enzyme activity is 125.0U/ml.
Lipase CALB is commercial lipases, and measuring enzyme activity is 150.0U/ml.
Embodiment 1
100g OCC oven dry stock is weighed, reduction paste is dense to 4%, and esterase EST1 additive amount is 0.2U/g (relative to over dry Slurry), treatment temperature is 40 DEG C, pH 5.0, handles time 45min, speed of agitator 100rpm, embodiment is according to TAPPIT- 277 gluing object measuring methods are screened slurry using Pulmac-MasterScreen pulp classifier, the gluing object that will be sifted out later It is dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object content after enzymatic treatment.It is being not added In the case where enzyme, secondary stock is handled with remaining the same terms, measuring result is blank group gluing object content.
Embodiment 2
100g OCC oven dry stock is weighed, reduction paste is dense to 5%, and esterase EST1 additive amount is 0.5U/g (relative to over dry Slurry), treatment temperature is 55 DEG C, pH 5.0, handles time 60min, speed of agitator 120rpm, embodiment is according to TAPPIT- 277 gluing object measuring methods are screened slurry using Pulmac-MasterScreen pulp classifier, the gluing object that will be sifted out later It is dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object content after enzymatic treatment.It is being not added In the case where enzyme, secondary stock is handled with remaining the same terms, measuring result is blank group gluing object content.
Embodiment 3
100g OCC oven dry stock is weighed, reduction paste is dense to 5%, and esterase EST1 additive amount is 0.5U/g (relative to over dry Slurry), treatment temperature is 55 DEG C, pH 7.0, handles time 60min, speed of agitator 120rpm, embodiment is according to TAPPIT- 277 gluing object measuring methods are screened slurry using Pulmac-MasterScreen pulp classifier, the gluing object that will be sifted out later It is dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object content after enzymatic treatment.It is being not added In the case where enzyme, secondary stock is handled with remaining the same terms, measuring result is blank group gluing object content.
Embodiment 4
100g OCC oven dry stock is weighed, reduction paste is dense to 5%, and esterase EST1 additive amount is 0.5U/g (relative to over dry Slurry), treatment temperature is 55 DEG C, pH 9.0, handles time 60min, speed of agitator 120rpm, embodiment is according to TAPPIT- 277 gluing object measuring methods are screened slurry using Pulmac-MasterScreen pulp classifier, the gluing object that will be sifted out later It is dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object content after enzymatic treatment.It is being not added In the case where enzyme, secondary stock is handled with remaining the same terms, measuring result is blank group gluing object content.
Embodiment 5
100g OCC oven dry stock is weighed, reduction paste is dense to 6%, and esterase EST1 additive amount is 1.0U/g (relative to over dry Slurry), treatment temperature is 80 DEG C, pH 7.0, handles time 120min, speed of agitator 150rpm, embodiment is according to TAPPIT- 277 gluing object measuring methods are screened slurry using Pulmac-Master Screen pulp classifier, the gluing that will be sifted out later Object dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object content after enzymatic treatment.Not In the case where enzyme, secondary stock is handled with remaining the same terms, measuring result is blank group gluing object content.
Comparative example 1
Lipase CALB, which is added, replaces esterase EST1 to handle secondary stock, and other conditions are same as Example 1, comparative example Slurry is screened using Pulmac-Master Screen pulp classifier according to TAPPIT-277 gluing object measuring method, later will The gluing object sifted out dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object after enzymatic treatment Content.In the case where not enzyme, secondary stock is handled with remaining the same terms, measuring result is that blank group gluing object contains Amount.
Comparative example 2
Lipase CALB, which is added, replaces esterase EST1 to handle secondary stock, and other conditions are same as Example 2, comparative example Slurry is screened using Pulmac-Master Screen pulp classifier according to TAPPIT-277 gluing object measuring method, later will The gluing object sifted out dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object after enzymatic treatment Content.In the case where not enzyme, secondary stock is handled with remaining the same terms, measuring result is that blank group gluing object contains Amount.
Comparative example 3
Lipase CALB, which is added, replaces esterase EST1 to handle secondary stock, and other conditions are same as Example 3, comparative example Slurry is screened using Pulmac-Master Screen pulp classifier according to TAPPIT-277 gluing object measuring method, later will The gluing object sifted out dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object after enzymatic treatment Content.In the case where not enzyme, secondary stock is handled with remaining the same terms, measuring result is that blank group gluing object contains Amount.
Comparative example 4
Lipase CALB, which is added, replaces esterase EST1 to handle secondary stock, and other conditions are same as Example 4, comparative example Slurry is screened using Pulmac-Master Screen pulp classifier according to TAPPIT-277 gluing object measuring method, later will The gluing object sifted out dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object after enzymatic treatment Content.In the case where not enzyme, secondary stock is handled with remaining the same terms, measuring result is that blank group gluing object contains Amount.
Comparative example 5
Lipase CALB, which is added, replaces esterase EST1 to handle secondary stock, and other conditions are same as Example 5, comparative example Slurry is screened using Pulmac-Master Screen pulp classifier according to TAPPIT-277 gluing object measuring method, later will The gluing object sifted out dyed, tabletting, finally carries out analysis scanning with scanning software, and then measure the gluing object after enzymatic treatment Content.In the case where not enzyme, secondary stock is handled with remaining the same terms, measuring result is that blank group gluing object contains Amount.
Table 1
As shown in Table 1, under the conditions of 40~55 DEG C, gluing object content in high temperature esterase EST1 treated secondary stock is added It significantly reduces, stickies removal rate will be substantially better than the removal effect of lipase CALB up to 58.9%~66.5%.Even if Under 80 DEG C of hot conditions, the treatment effect after esterase EST1 is added is also ideal, and the stickies removal rate in secondary stock reaches 54.1%, and lipase CALB is inactivated substantially with this condition, it is difficult to remove gluing object.In view of different in paper-making process from waste paper The temperature of workshop section is not quite similar, and esterase EST1 is ideal in the effect that waste paper recycles removal gluing object in different workshop sections.

Claims (1)

1. a kind of method using gluing object in high temperature esterase removal secondary stock, it is characterised in that include the following steps:
The preparation process of esterase EST1: using the encoding gene for the EST1 esterase that full genome synthetic method obtains, and it is cloned into table Recombinant expression carrier is obtained on up to carrier pET23a-CBD carrier, utilizes CaCl2Conversion method will contain EST1 esterase encoding gene Expression plasmid be transferred in BL21 (DE3) strain, obtain genetic engineering bacterium, the strain of esterase EST1 is connected to containing Amp100ug/ Expand culture in the LB seed culture medium of ml, when OD value reaches 0.6~0.8, bacterium solution is inoculated into according to the ratio of 1:100 and is contained In the LB fermentation medium of Amp100ug/ml, shake to OD value be 0.6~0.8 when be added 20mmol/L IPTG inducer carry out Inducing expression, 18~receive bacterium afterwards for 24 hours, collecting pipe parietal cell surpasses after bacterium solution is centrifuged 10min under the conditions of 12000r/min Sound is broken, and later again to take supernatant to get to crude enzyme liquid after 12000r/min pelleted by centrifugation 10min, it is fine that 1L bacterium solution corresponds to 1g Dimension is plain, and by crude enzyme liquid, 30min, in due course stirring in conjunction with rear high speed centrifugation 10min, discard supernatant liquid in conjunction with cellulose under room temperature, Adhesion protein is washed twice with PBS buffer solution, HRV 3CP is first being centrifuged before, is discarding supernatant, and is cleaned using PBS buffer solution 2 times, appropriate PBS is added into adhesion protein, digestion 4h or overnight after being mixed in the ratio that 1L bacterium solution corresponds to 1ml HRV 3CP, High speed centrifugation after digestion, supernatant are pure enzyme;
100g OCC oven dry stock is weighed, reduction paste is dense to 6%, and esterase EST1 additive amount is 1.0U/g (relative to oven dry stock matter Amount), treatment temperature is 80 DEG C, pH 7.0, handles time 120min, speed of agitator 150rpm.
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Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN101220567A (en) * 2008-01-24 2008-07-16 广东轻工职业技术学院 Method for controlling with 100aste newsprint paper deinked pulp esterase
CN104781398A (en) * 2012-10-26 2015-07-15 罗尔公司 Novel esterases in the treatment of cellulosic and lignocellulosic material

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN101220567A (en) * 2008-01-24 2008-07-16 广东轻工职业技术学院 Method for controlling with 100aste newsprint paper deinked pulp esterase
CN104781398A (en) * 2012-10-26 2015-07-15 罗尔公司 Novel esterases in the treatment of cellulosic and lignocellulosic material

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
Crystal structure of hyperthermophilic esterase EstE1 and the;Jung-Sue Byun etal.;<<BMC Structural Biology>>;20070712;第7卷(第47期);1-11

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