α-Amylases (E.C 3.2.1.1) hydrolyse starch into smaller moieties such as maltose and glucose by breaking α-1,4-glycosidic linkages. The application of α-amylases in various industries has made the large-scale productions of these enzymes crucial. Thermostable α-amylase that catalyses starch degradation at the temperatures higher than 50 °C is favourable in harsh industrial applications. Due to ease in genetic manipulation and bulk production, this enzyme is most preferably produced by microorganisms. Bacillus sp. and Escherichia coli are commonly used microbial expression hosts for α-amylases (30 to 205 kDa in molecular weight). These amylases can be purified using ultrafiltration, salt precipitation, dialysis, and column chromatography. Recently, affinity column chromatography has shown the most promising result where the recovery rate was 38 to 60% and purification up to 13.2-fold. Microbial thermostable α-amylases have the optimum temperature and pH ranging from 50 °C to 100 °C and 5.0 to 10.5, respectively. These enzymes have high specificity towards potato starch, wheat starch, amylose, and amylopectin. EDTA (1 mM) gave the highest inhibitory effect (79%), but Ca2+ (5 mM) was the most effective co-factor with 155%. This review provides insight regarding thermostable α-amylases obtained from microbial sources for industrial applications.

Purpose This paper aims to measure mean voluntary intellectual capital disclosure (ICD) quality score for a sample of Australian Stock Exchange-listed biotechnology firms in the 2003, 2006 and 2010 reporting periods. The aim was to use data for the same companies over the whole period to discover whether the quality of voluntary reporting practice was improving over time, measuring lagged-mean ICD quality score against possible determinants of management disclosure practice. Design/methodology/approach Mean ICD quality score, and associated frequency data, was measured against possible determinants of managers’ disclosure practice. The dependent variable was an 18-item classification of ICD based on Sveiby’s Intangible Assets Monitor (Sveiby, 1997). Data collected from S&P Capital IQ database were used to compare ICD disclosure quality with possible drivers: competition (capital intensity); performance (profit and market returns); monitoring (audit firm and ownership); and control variables (revenue and leverage). Findings Mean voluntary disclosures of internal capital and external capital lower the quality over time using paired sample t-test comparison against 2003 as a base year. The lowest quality disclosure was about human capital, and the highest quality was about internal capital. Individual disclosure items within internal, external and human capital classification showed that internal capital items (intellectual property, corporate culture, management processes and financial relations) and external capital item (customers) were the significant contributors. Investigation of drivers using Spearman’s correlation against lagged ICD data showed that performance (relative market returns) and monitoring (ownership diffusion) were significant drivers of voluntary ICD, both in expected and unexpected ways. Originality/value Voluntary ICD quality and quantity are rarely measured in the same paper. The findings are unique and interesting especially for innovative Australian R&D firms when compared to recent findings for a larger sample of French companies.

Background α-amylases catalyze the endo-hydrolysis of α-1,4-D-glycosidic bonds in starch into smaller moieties. While industrial processes are usually performed at harsh conditions, α-amylases from mainly the bacteria, fungi and yeasts are preferred for their stabilities (thermal, pH and oxidative) and specificities (substrate and product). Microbial α-amylases can be purified and characterized for industrial applications. While exploring novel enzymes with these properties in the nature is time-costly, the advancements in protein engineering techniques including rational design, directed evolution and others have privileged their modifications to exhibit industrially ideal traits. However, the commentary on the strategies and preferably mutated residues are lacking, hindering the design of new mutants especially for enhanced substrate specificity and oxidative stability. Thus, our review ensures wider accessibility of the previously reported experimental findings to facilitate the future engineering work. Survey methodology and objectives A traditional review approach was taken to focus on the engineering of microbial α-amylases to enhance industrially favoured characteristics. The action mechanisms of α- and β-amylases were compared to avoid any bias in the research background. This review aimed to discuss the advances in modifying microbial α-amylases via protein engineering to achieve longer half-life in high temperature, improved resistance (acidic, alkaline and oxidative) and enhanced specificities (substrate and product). Captivating results were discussed in depth, including the extended half-life at 100 °C, pH 3.5 and 10, 1.8 M hydrogen peroxide as well as enhanced substrate (65.3%) and product (42.4%) specificities. These shed light to the future microbial α-amylase engineering in achieving paramount biochemical traits ameliorations to apt in the industries. Conclusions Microbial α-amylases can be tailored for specific industrial applications through protein engineering (rational design and directed evolution). While the critical mutation points are dependent on respective enzymes, formation of disulfide bridge between cysteine residues after mutations is crucial for elevated thermostability. Amino acids conversion to basic residues was reported for enhanced acidic resistance while hydrophobic interaction resulted from mutated hydrophobic residues in carbohydrate-binding module or surface-binding sites is pivotal for improved substrate specificity. Substitution of oxidation-prone methionine residues with non-polar residues increases the enzyme oxidative stability. Hence, this review provides conceptual advances for the future microbial α-amylases designs to exhibit industrially significant characteristics. However, more attention is needed to enhance substrate specificity and oxidative stability since they are least reported.

Candidiasis is a fungal infection caused by Candida spp. especially Candida albicans, C. glabrata, C. parapsilosis and C. tropicalis. Although the medicinal therapeutic strategies have rapidly improved, the mortality rate due to candidiasis has continuously increased. The secreted and membrane-bound virulence factors (VFs) are responsible for fungal invasion, damage and translocation through the host enterocytes besides the evasion from host immune system. VFs such as agglutinin-like sequences (Als), heat shock protein 70, phospholipases, secreted aspartyl proteinases (Sap), lipases, enolases and phytases are mostly hydrolases which degrade the enterocyte membrane components except for candidalysin, the VF acts as a peptide toxin to induce necrotic cell lysis. To date, structural studies of the VFs remain underexplored, hindering their functional analyses. Among the VFs, only secreted aspartyl proteinases and agglutinin-like sequences have their structures deposited in Protein Data Bank (PDB). Therefore, this review scrutinizes the mechanisms of these VFs by discussing the VF-deficient studies of several Candida spp. and their abilities to produce these VFs. Nonetheless, their latest reported sequential and structural analyses are discussed to impart a wider perception of the host-pathogen interactions and potential vaccine or antifungal drug targets. This review signifies that more VFs structural investigations and mining in the emerging Candida spp. are required to decipher their pathogenicity and virulence mechanisms compared to the prominent C. albicans. Lay Abstract Candida virulence factors (VFs) including mainly enzymes and proteins play vital roles in breaching the human intestinal barrier and causing deadly candidiasis. Limited VFs’ structural studies hinder deeper comprehension of their mechanisms and thus the design of vaccines and antifungal drugs against fungal infections.

Pasteurella spp. are Gram-negative facultative bacteria that cause severe economic and animal losses. Pasteurella-based vaccines are the most promising solution for controlling Pasteurella spp. outbreaks. Remarkably, insufficient biomass cultivation (low cell viability and productivity) and lack of knowledge about the cultivation process have impacted the bulk production of animal vaccines. Bioprocess optimization in the shake flask and bioreactor is required to improve process efficiency while lowering production costs. However, its state of the art is limited in providing insights on its biomass upscaling, preventing a cost-effective vaccine with mass-produced bacteria from being developed. In general, in the optimum cultivation of Pasteurella spp., production factors such as pH (6.0–8.2), agitation speed (90–500 rpm), and temperature (35–40 °C) are used to improve production yield. Hence, this review discusses the production strategy of Pasteurella and Mannheimia species that can potentially be used in the vaccines for controlling pasteurellosis. The physicochemical factors related to operational parameter process conditions from a bioprocess engineering perspective that maximize yields with minimized production cost are also covered, with the expectation of facilitating the commercialization process.