Enzyme & Microbial Technology Research Center - EMTech

The research group was first established in 1986 and has developed into a model integrated research group.

The Enzyme and Microbial Technology Research Centre (EMTech), Universiti Putra Malaysia was established in 2012 as a natural progression in the development of a highly successful research group. Extensive work has been conducted on isolation and identification of microorganisms producing enzymes and peptides that are useful for industrial applications, as well as utilizing some isolates as potenti

06/08/2024

Congratulations to our EMTech researchers; Prof. Dr. Mohd Shukuri Bin Mohamad Ali, Assoc. Prof. Dr. Adam Leow Thean Chor, Assoc. Prof. Dr. Siti Nurbaya Binti Oslan, Assoc. Prof. Dr. Suriana Binti Sabri, Dr. Noor Dina Binti Muhd Noor and Dr. Nor Hafizah Binti Ahmad Kamarudin, upon receiving the Journal Publication Initiative 2024 totaling at RM 86,000 !!

Photos from Enzyme & Microbial Technology Research Center - EMTech's post 05/08/2024

From July 29 to July 31, 2024, EMTech welcomed representatives Dr. Fathoni, Dr. Andi, and Dr. Dede from the Applied Microbiology Research Center, Badan Riset dan Inovasi Nasional (BRIN), Indonesia. A number of topics were discussed between the two sides, including potential research collaboration between EMTech and BRIN for the structural biology platform, research funds, visiting researcher programs, and opportunities for training and seminars. They also visited the Institute of Bioscience and other research laboratories at UPM, and took a tour of the Malaysia Genome and Vaccine Institute (MGVI), Bangi.

24/07/2024

CONGRATULATIONS TO EMTECH'S PROUD RECEIVERS OF THE PRESTIGIOUS FRGS 2024

Congrats Prof. Madya Dr. Normi on:

Grant received: RM 177,600
Project title: Rational design and characterization of effective, novel, cross-class peptide inhibitors against New Delhi B1 and BLEG-1 B3 metallo-B-lactamase to tackle antimicrobial resistance.

Congrats Prof. Madya Dr. Siti Nurbaya Oslan on:

Grant received: RM 154,800
Project title: Investigation into Critical Mutation Hotspot in Newly Designed Microbial Lipase for Cheese Flavour Enhancement from Short-chain Triglyceride in Buffalo Milk

Photos from Research Management Centre UPM's post 23/07/2024
Photos from Enzyme & Microbial Technology Research Center - EMTech's post 12/07/2024

On the 11th of July our Head of Enzyme & Microbial Technology Research Center - EMTech Prof. Dr. Mohd Shukuri Mohamad Ali presented a talk on "Structural Biology As A Powerful Tool In Modern Microbiology" for the The Joint Academic Microbiology Seminars (JAMS) Kuala Lumpur in collaboration with the Malaysian Society for Microbiology (MSM) July Seminar 2024.

This event brought together esteemed researchers and scientists from all walks of life to connect on the latest discoveries in science. It was great to see everyone's enthusiasm as we connected over lunch at Padi House, Ioi conezion putrajaya serdang.

Looking forward to the next time! Thank you all for attending.

12/07/2024

Check out our recent article on 'Extracellular BSA-degrading SAPs in the rare pathogen Meyerozyma guilliermondii strain SO as potential virulence factors in candidiasis' now available online at:

https://doi.org/10.1016/j.micpath.2024.106773

Here is the summary:
Secreted aspartyl proteinases (SAPs) remain one of the prominent virulence factors in Candida species that cause candidiasis. While Meyerozyma guilliermondii strain SO could express industrially important enzymes, the current findings indicated that MgSAPs were produced in the nitrogen-limited medium with BSA as the sole nitrogen source by both planktonic and biofilm cells. While no SAP activity was detected in avirulent Saccharomyces cerevisiae, MgSAPs cleaved BSA for nutrient acquisition and growth besides showing a similar cleavage profile with HIV-1 retropepsin. This study highlighted the pathogenicity of M. guilliermondii strain SO through its MgSAP production and their potential as antifungal drug targets.

Congratulations to all authors; Si Jie Lim, Noor Dina Muhd Noor, Suriana Sabri, Mohd Shukuri Mohamad Ali, Abu Bakar Salleh, Siti Nurbaya Oslan !

Redirecting

Antimicrobial peptides from Bacillus spp. and strategies to enhance their yield - PubMed 04/06/2024

Check out our recent article on 'Antimicrobial peptides from Bacillus spp. and strategies to enhance their yield' now available online at:

https://pubmed.ncbi.nlm.nih.gov/37450018/

Here's the summary:

Antibiotic resistance is a growing global concern, which arises primarily due to overuse of antibiotics. Therefore, searching alternative solutions to tackle this problem is crucial. This review provides a comprehensive understanding of antimicrobial peptides (AMPs) produced by Bacillus species, which show promise as alternatives to traditional antibiotics. It summarizes different categories of AMPs, their antimicrobial spectrum, mode of actions, potential industrial applications and key biosynthetic gene clusters. Furthermore, this review discusses various approaches to increase the yield of AMPs, such as culture medium optimization and genetic engineering. In overall, this review offers valuable insights for researchers to develop cost-effective and scalable methods for large-scale production of Bacillus-derived AMPs, aiming to combat the emerging antibiotic resistance.

Congratulations to all authors; Sheau Ling Puan, Pirasannah Erriah, Mohamad Malik Al-Adil Baharudin, Normi Mohd Yahaya, Wan Nur Ismah Wan Ahmad Kamil, Mohd Shukuri Mohamad Ali, Siti Aqlima Ahmad, Siti Nurbaya Oslan, Sooa Lim, Suriana Sabri

Antimicrobial peptides from Bacillus spp. and strategies to enhance their yield - PubMed Antibiotic resistance is a growing concern that is affecting public health globally. The search for alternative antimicrobial agents has become increasingly important. Antimicrobial peptides (AMPs) produced by Bacillus spp. have emerged as a promising alternative to antibiotics, due to their broad-s...

Not found - PubMed 29/05/2024

Check out our recent article on 'Thermodynamics of a hyperthermostable carboxylesterase from Anoxybacillus geothermalis D9' now available online at:

https://pubmed.ncbi.nlm.nih.gov/38621445/https://pubmed.ncbi.nlm.nih.gov/38621445/

Here's the summary:

Hyperthermostable enzymes, like EstD9 from Anoxybacillus geothermalis D9, offer exceptional stability in extreme temperatures, making them valuable biocatalysts. This study explores EstD9 conformational adaptability at high temperatures, revealing the emergence of new β-sheets crucial to its hydrolase structure. Molecular dynamics simulations demonstrate its compact arrangement and the protective role of three loops around its catalytic site. Further analysis uncovers extensive intramolecular interactions, surpassing the homolog protein structure, Est30. These findings highlight the significance of these interactions and structural dynamics in maintaining EstD9 integrity at high temperatures, suggesting its potential as a valuable industrial enzyme.

Congratulations to all authors; Ummie Umaiera Mohd Johan, Raja Noor Zaliha Raja Abd Rahman, Nor Hafizah Ahmad Kamarudin, Mohd Shukuri Mohamad Ali

Not found - PubMed The .gov means it’s official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Photos from Enzyme & Microbial Technology Research Center - EMTech's post 17/05/2024

Selamat Hari Raya!

On the 7th of May 2024 we celebrated the joy, love and blessings of Eid with our Annual EMTech Raya 2024 event. Scroll through to relive our special moments and memories of the day which were filled with peace and laughter. May this Eid bring us happiness, prosperity and may we gather again next time!

08/05/2024

Enzyme and Microbial Technology Research Centre Releases 2023 Annual Report

The Enzyme and Microbial Technology Research Centre is proud to announce the publication of its 2023 Annual Report, detailing a year of notable achievements and significant advancements in enzyme and microbial research. Established in 1986 and a cornerstone of academic and practical research excellence, the centre continues to lead with groundbreaking findings and substantial contributions to the field.

This year’s report highlights the centre's successful acquisition of RM 1,840,461 in research grants, the prolific output of 37 scholarly articles—with an impressive 97.3% indexed in citation databases and nearly 60% in top-tier Top 10%, Q1 and Q2 journals—and the dynamic involvement in 27 international and national conferences.

You can access the annual report by visiting the URL: www.emtech.upm.edu.my

Carboxylic acid reductases: Structure, catalytic requirements, and applications in biotechnology - PubMed 26/04/2024

Check out our recent article on 'Carboxylic acid reductases: Structure, catalytic requirements, and applications in biotechnology' now available online at:

https://pubmed.ncbi.nlm.nih.gov/37080403/ #:~:text=Carboxylic%20acid%20reductases%20(CARs)%20are,adenine%20dinucleotide%20phosphate%20(NADPH)

Here's the summary:

Scientists are excited about biocatalysts, natural tools that can make industrial processes cleaner. This review focuses on carboxylic acid reductases (CARs), found in bacteria and fungi. These large protein molecules turn carboxylic acids (abundant in nature) into aldehydes, useful for various products like vanillin. The article explores how CARs work, including their structure, how they require activation, and how the enzymes are being improved. This research could lead to cleaner industrial processes in the future.

Congratulations to all authors; Rose Syuhada Basri, Raja Noor Zaliha Raja Abd Rahman, Nor Hafizah Ahmad Kamarudin, Mohd Shukuri Mohamad Ali !

Carboxylic acid reductases: Structure, catalytic requirements, and applications in biotechnology - PubMed Biocatalysts have been gaining extra attention in recent decades due to their industrial-relevance properties, which may hasten the transition to a cleaner environment. Carboxylic acid reductases (CARs) are large, multi-domain proteins that can catalyze the reduction of carboxylic acids to correspon...

Photos from Enzyme & Microbial Technology Research Center - EMTech's post 01/04/2024

On the 27th of March 2024, Enzyme & Microbial Technology Research Center - EMTech had our Annual Iftar Programme 2024 which was attended by all P*s, students and family. It was a wonderful event blessed by prayers, food/drink and good company. Thank you to all who have contributed and attended this event and may we continue to gather in the years to come. Ramadhan Mubarak to all 💐💕

Molecular dynamics simulation and structural analysis of aquaporin Z from an Antarctic Pseudomonas sp. strain AMS3 26/03/2024

Check out our recent article on 'Molecular dynamics simulation and structural analysis of aquaporin Z from an Antarctic Pseudomonas sp. strain AMS3' now available online at:

https://www.tandfonline.com/doi/abs/10.1080/07391102.2022.2164519

Here's a short summary:
This article introduces the aquaporin (AQP) protein, a crucial element in facilitating water movement across cell membranes. Despite its ubiquity, understanding its mechanisms in microbes adapted to low temperatures and its potential industrial applications has been limited. To address this, the study focuses on expressing, extracting, purifying, and studying the aquaporin Z family from Pseudomonas sp. AMS3. Through molecular approaches, particularly with the AqpZ1 AMS3 gene, the research successfully expressed and optimized the protein's conditions, shedding light on its structural adaptations at low temperatures and its potential for molecular engineering and industrial applications in the future.

Congratulations to all authors ; S. Balakrishnan, R. N. Z. R. A. Rahman, N. D. M. Noor, W. Latip and M.S.M Ali !

Molecular dynamics simulation and structural analysis of aquaporin Z from an Antarctic Pseudomonas sp. strain AMS3 Aquaporin is a water channel protein that facilitates the movement of water across the cell membrane. Aquaporin from the Antarctic region has been noted for its psychrophilic properties and its abi...

25/03/2024

Congratulations to our researchers for achieving the top downloaded article within its first 12 months of publication! Explore the review paper on the versatility of subtilisin in our article published in Biotechnology and Applied Biochemistry. Check it out here: https://doi.org/10.1002/bab.2309

Enolase in Meyerozyma guilliermondii strain SO: Sequential and structural insights of MgEno4581 as a putative virulence factor and host-fungal interactions through comprehensive in silico approaches - PubMed 15/03/2024

Check out our recent article on 'Enolase in Meyerozyma guilliermondii strain SO: Sequential and structural insights of MgEno4581 as a putative virulence factor and host-fungal interactions through comprehensive in silico approaches' now available online at:

https://pubmed.ncbi.nlm.nih.gov/36754101/

Here's a short summary:
Enolase is the biomarker for candidiasis. As a moonlighting protein, it performs various functions including enzymatic activities (transglutaminase and lyase) and binding to the human extracellular matrix proteins to elicit pathogenicity. Here, the enolase of rare pathogen Meyerozyma guilliermondii was identified. The protein-protein docking between fungal/yeast enolases with human plasminogen (HPG) predicted that the interaction of enolase from pathogenic Candida albicans with HPG was more conserved in M. guilliermondii compared to avirulent Saccharomyces cerevisiae. Future in vitro and in vivo studies can be performed to validate the prediction and elucidate its roles in the pathogenicity of M. guilliermondii.

Congratulations to all authors ; Alia Iwani Amran, Si Jie Lim, Noor Dina Muhd Noor, Abu Bakar Salleh, Siti Nurbaya Oslan !

Enolase in Meyerozyma guilliermondii strain SO: Sequential and structural insights of MgEno4581 as a putative virulence factor and host-fungal interactions through comprehensive in silico approaches - PubMed Meyerozyma guilliermondii is a rare opportunistic fungal pathogen that causes deadly invasive candidiasis in human. M. guilliermondii strain SO is a local yeast isolate that possesses huge industrial interests but also pathogenic towards zebrafish embryos. Enolases that bind to human extracellular m...

Photos from Enzyme & Microbial Technology Research Center - EMTech's post 22/02/2024

Special guest at the Biotech Seminar (FBSB) series 12/2024 organized by Enzyme & Microbial Technology Research Center - EMTech. 🌟Dr. Bergfors, an expert in protein crystallization, impressed us with her talk and shared insights from her work at the Uppsala Crystallization Platform (Uppsala University, Sweden). A big thank you to everyone who joined us and shared the excitement!!

02/02/2024

Enzyme & Microbial Technology Research Center - EMTech cordially invites you to the Biotech Seminar:

Structure and Function of Disease-related Human Membrane Proteins by Professor Dr. Weontae Lee

Trafficking, Secretion and Display of Homologous Proteins and Fusion Proteins in Lactococcus lactis by Assoc. Prof. Dr. Clemens Peterbauer

Date: 21st February 2024
Venue: Bilik Seminar 1.4 FBSB

Join us for this exciting event and register now!

02/02/2024

Enzyme & Microbial Technology Research Center - EMTech cordially invites you to the Biotech Seminar by Dr. Terese Bergfors on Looking for Needles in A Haystack: Protein Crystallisation Strategies for A Drug-discovery Program.

Date: 7th February 2024
Venue: Bilik Seminar 1.4 FBSB

Register now at the QR code below. See you there!

23/01/2024

"Teamwork makes the dream work! 🌐✨ Here's to our very first quarterly meeting – a snapshot of dedication and excellence. Excited for a more productive year ahead and embracing new goals together! 💪🔬

Worldwide trend discovery of structural and functional relationship of metallo-β-lactamase for structure-based drug design: A bibliometric evaluation and patent analysis 17/01/2024

Check out our recent article on 'Worldwide trend discovery of structural and functional relationship of metallo-β-lactamase for structure-based drug design: A bibliometric evaluation and patent analysis' now available online at: https://www.sciencedirect.com/science/article/abs/pii/S0141813023051292

Here's a short summary:

This article explores the global research trends on Metallo-β-lactamase (MBL), an enzyme produced by bacteria that can deactivate many antibiotics, posing a threat to effective infection treatment and increasing antibiotic resistance. The study, conducted from 2013 to 2022, uses bibliometric and patent analyses to evaluate MBL research. Key findings highlights the importance of exploring the structural and functional aspects of MBL for developing effective drugs to counter antibiotic-resistant bacterial infections.

Congratulations to all authors ; Ameera Aisyah Azman, Adam Thean Chor Leow, Noor Dina Muhd Noor, Siti Aminah Mohd Noor, Wahhida Latip, Mohd Shukuri Mohamad Ali !

Worldwide trend discovery of structural and functional relationship of metallo-β-lactamase for structure-based drug design: A bibliometric evaluation and patent analysis Metallo-β-lactamase (MBL) is an enzyme produced by clinically important bacteria that can inactivate many commonly used antibiotics, making them a sig…

Photos from Enzyme & Microbial Technology Research Center - EMTech's post 15/01/2024

Snippets from our fellow EMTech representatives who welcomed and introduced the Enzyme & Microbial Technology Research Center - EMTech to visiting form 5 and form 6 students from SMK Shing Chung, Perak. The students were shown around the lab and got to know some of the cool and exciting projects that EMTech are involved in 👍🏻

Photos from Enzyme & Microbial Technology Research Center - EMTech's post 12/01/2024

Heartiest congratulations to Lim Si Jie (CJ) on passing his PhD Viva with distinction! We are proud of you and may this serve to motivate us that hard work indeed pays off 💪🏻

Features of the rare pathogen Meyerozyma guilliermondii strain SO and comprehensive in silico analyses of its adherence-contributing virulence factor agglutinin-like sequences 11/01/2024

Congratulations, we’re delighted to let you know that the final published article (the Version of Record) is now on Taylor & Francis Online.

Summary:
In this study, we reported on the pathogenicity in Meyerozyma guilliermondii (Candida guilliermondii) that was isolated from spoilt orange (SO). Although this fungus can cost-efficiently produce industrially important enzymes (lipase, amylase, protease, and diamine oxidase), our study showed its higher tolerance towards many stresses, biofilm mass, and mortality (zebrafish embryos) compared to the safe Baker yeast. To understand its pathogenicity, we identified and analyzed comprehensively the adhesin protein in M. guilliermondii strain SO. Our results predicted that one (MgAls1056) of them was critical for its fungal pathogenicity and a promising antifungal drug target. This study signified the safety concerns of microbial usage in industries and the powerful computational tools to identify and characterize the adhesin proteins in Candida species.

Authors: Si Jie Lim ,Noor Dina Muhd Noor ,Suriana Sabri ,Mohd Shukuri Mohamad Ali ,Abu Bakar Salleh &Siti Nurbaya Oslan
Received: 25 Jul 2023
Accepted:17 Dec 2023
Published online: 08 Jan 2024

To cite this article:

Features of the rare pathogen Meyerozyma guilliermondii strain SO and comprehensive in silico analyses of its adherence-contributing virulence factor agglutinin-like sequences Meyerozyma guilliermondii is a rare yeast pathogen contributing to the deadly invasive candidiasis. M. guilliermondii strain SO, as a promising protein expression host, showed 99% proteome similari...

02/05/2023

Our review article on "Carboxylic acid reductases: Structure, catalytic requirements, and applications in biotechnology" was recently published in the International Journal of Biological Macromolecules".

In this comprehensive review, we summarize the previous findings on the phylogeny, structural and mechanical insight of the domains, post-translational modification requirement, strategies for the cofactors regeneration, the extensively broad aldehyde-related industrial application properties of CARs, as well as their recent immobilization approaches.

Have a read via this link:
https://doi.org/10.1016/j.ijbiomac.2023.124526
https://www.sciencedirect.com/science/article/pii/S0141813023014204?via%3Dihub

Congratulations to all authors.
Rose Syuhada Basri, Prof. Dr. Raja Noor Zaliha Raja Abd. Rahman, Dr. Nor Hafizah Ahmad Kamarudin, and Assoc. Prof. Dr. Mohd Shukuri Mohamad Ali.

Redirecting

Immobilization of Hyperthermostable Carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer Material and Its Physicochemical Properties 02/05/2023

A new article on the "Immobilization of Hyperthermostable Carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer Material and Its Physicochemical Properties" published in Polymers is now available online.

https://doi.org/10.3390/polym15061361

The study aimed to immobilize hyperthermostable carboxylesterase from Anoxybacillus geothermalis D9 with improved stability and reusability. Through immobilization, the enzyme demonstrates the improvement of the operational stability and properties for better practical applications.

Congratulations to all authors,
Ummie Umaiera Mohd. Johan, Prof Dr. Raja Noor Zaliha Raja Abd. Rahman, Dr. Nor Hafizah Ahmad Kamarudin, Dr. Wahhida Latip and Assoc. Prof. Dr. Mohd Shukuri Mohamad Ali.

https://www.mdpi.com/2073-4360/15/6/1361

Immobilization of Hyperthermostable Carboxylesterase EstD9 from Anoxybacillus geothermalis D9 onto Polymer Material and Its Physicochemical Properties Carboxylesterase has much to offer in the context of environmentally friendly and sustainable alternatives. However, due to the unstable properties of the enzyme in its free state, its application is severely limited. The present study aimed to immobilize hyperthermostable carboxylesterase from Anox...

Molecular dynamics simulation and structural analysis of aquaporin Z from an Antarctic Pseudomonas sp. strain AMS3 28/03/2023

Membrane proteins are indeed interesting biocatalysts.
Our new research article on "Molecular dynamics simulation and structural analysis of aquaporin Z from an Antarctic Pseudomonas sp. strain AMS3" has been published in the Journal of Biomolecular Structure and Dynamics. To gain insight into membrane proteins, check out this article.

https://doi.org/10.1080/07391102.2022.2164519

Congratulations to all authors!
Samyuktha Balakrishnan, Prof Dr. Raja Noor Zaliha Raja Abd. Rahman, Dr. Noor Dina Muhd Noor, Dr. Wahhida Latip and corresponding author, AP Dr. Mohd Shukuri Mohamad Ali.

Molecular dynamics simulation and structural analysis of aquaporin Z from an Antarctic Pseudomonas sp. strain AMS3 Aquaporin is a water channel protein that facilitates the movement of water across the cell membrane. Aquaporin from the Antarctic region has been noted for its psychrophilic properties and its abi...

23/03/2023

Ramadhan Kareem everyone!
May the holy month of Ramadhan shower us with the best blessings and bring eternal joy in life.

Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues 14/12/2022

A new review article on "Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues" published in the International Journal of Molecular Sciences is now available online.

Do check out and have a read via this link,
https://doi.org/10.3390/ijms232315394

The current review looked at the recombinant overexpression, purification, and recent mechanism of cold adaptation, various approaches for purification, and three-dimensional (3D) crystal structure elucidation of cold-active lipases and esterase.

https://www.mdpi.com/1422-0067/23/23/15394

Congratulations to all authors
Adamu Idris Matinja, Dr. Nor Hafizah Ahmad Kamarudin, AP Dr. Adam Thean Chor Leow, AP Dr. Siti Nurbaya Oslan, and AP Dr. Mohd Shukuri Mohamad Ali.

Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues Cold environments characterised by diverse temperatures close to or below the water freezing point dominate about 80% of the Earth’s biosphere. One of the survival strategies adopted by microorganisms living in cold environments is their expression of cold-active enzymes that enable them to pe...

16/11/2022

Congratulations to our EMTech researchers who recognized as World's Top 2% Scientist.
1. Prof. Dato' Dr. Abu Bakar Bin Salleh
11. Late Prof. Dr. Mahiran Binti Basri
20. Prof. Dr. Raja Noor Zaliha Binti Raja Abd Rahman

Membrane fatty acid desaturase: biosynthesis, mechanism, and architecture - Applied Microbiology and Biotechnology 15/11/2022

A new review article on "Membrane fatty acid desaturase: biosynthesis, mechanism, and architecture" is now available online.

This review serves to introduce the properties, mechanism and structural feature of membrane fatty acid desaturase. The understanding of this protein from the molecular basis is important for the advancement of therapeutic strategies related to the improvement of health issues.

Congratulations to all authors,
Nur Farah Anis Abd Halim, AP Dr. Mohd Shukuri Mohamad Ali, AP Dr. Adam Thean Chor Leow and Prof. Dr. Raja Noor Zaliha Raja Abd Rahman.

Membrane fatty acid desaturase: biosynthesis, mechanism, and architecture - Applied Microbiology and Biotechnology Abstract Fatty acid desaturase catalyzes the desaturation reactions by inserting double bonds into the fatty acyl chain, producing unsaturated fatty acids, which play a vital part in the synthesis of polyunsaturated fatty acids. Though soluble fatty acid desaturases have been described extensively i...

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